1.

Phenylphosphate synthase-Phenylphosphate synthase consists of three proteins whose genes are located adjacent to each other on the phenol operon and were overproduced in Escherichia coli. The promoter region and operon structure of the phenol gene cluster were investigated. Protein 1 (70 kDa) resembles the central part of classical phosphoenolpyruvate synthase which contains a conserved histidine residue. It catalyzes the exchange of free [(14)C]phenol and the phenol moiety of phenylphosphate but not the phosphorylation of phenol. Phosphorylation of phenol requires protein 1, MgATP, and another protein, protein 2 (40 kDa), which resembles the N-terminal part of phosphoenol pyruvate synthase. Proteins 1 and 2 catalyze the following reaction: phenol + MgATP + H(2)O-->phenylphosphate + MgAMP + orthophosphate. The phosphoryl group in phenylphosphate is derived from the beta-phosphate group of ATP. The free energy of ATP hydrolysis obviously favors the trapping of phenol (K(m), 0.04 mM), even at a low ambient substrate concentration. The reaction is stimulated severalfold by another protein, protein 3 (24 kDa), which contains two cystathionine-beta-synthase domains of unknown function but does not show significant overall similarity to known proteins. The molecular and catalytic features of phenylphosphate synthase resemble those of phosphoenolpyruvate synthase, albeit with interesting modifications. Pathway:

2.

Protein-Blast of phenylphosphate synthase subunit gamma [Geobacter metallireducens

GS-15] with genome of planococcus antarcticus. Query-enzyme sequence Reference-Planococcus Antarcticus genome seq

P Blast- putative phenylphosphate synthase PpsB [Clostridia bacterium enrichment culture clone BF]

P-Blast phenylphosphate synthase, beta subunit [Geobacter metallireducens GS-15]

P-Blast phenylphosphate synthase, alpha subunit [Geobacter metallireducens GS-15]

2) Phenyl phosphate carboxylase- This enzyme consists of four proteins with molecular masses of 54, 53, 18, and 10 kDa, whose genes are located adjacent to each other in the phenol gene cluster which codes for phenolinduced proteins. Three of the subunits (54, 53, and 10 kDa) were sufficient to catalyze the exchange of 14CO2 and the carboxyl group of 4-hydroxybenzoate but not phenylphosphate carboxylation. Phenylphosphate carboxylation was restored when the 18-kDa subunit was added. The following reaction model is proposed. The 14CO2 exchange reaction catalyzed by the three subunits of the core enzyme requires the fully reversible release of CO2 from 4-hydroxybenzoate with formation of a tightly enzyme-bound phenolate intermediate. Carboxylation of phenylphosphate requires in addition the 18-kDa subunit, which is thought to form the same enzyme-bound energized phenolate intermediate from phenylphosphate with virtually irreversible release of phosphate. The 54- and 53-kDa subunits show similarity to UbiD of Escherichia coli, which catalyzes the decarboxylation of a 4-hydroxybenzoate derivative in ubiquinone (ubi) biosynthesis. They also show similarity to components of various decarboxylases acting on aromatic carboxylic acids, such as 4-hydroxybenzoate or vanillate, whereas the 10-kDa subunit is unique. The 18-kDa subunit belongs to a hydratase/phosphatase protein family. Phenylphosphate carboxylase is a member of a new family of carboxylases/decarboxylases that act on phenolic compounds, use CO2 as a substrate, do not contain biotin or thiamine diphosphate, require K+ and a divalent metal cation (Mg2+or Mn2+) for activity, and are strongly inhibited by oxygen. P-Blast-phenylphosphate carboxylase, beta subunit [Geobacter metallireducens RCH3]

P-Blast-alpha subunit of phenylphosphate carboxylase [Aromatoleum aromaticum EbN1]

P-Blast-putative phenylphosphate carboxylase, gamma subunit [delta proteobacterium NaphS2]

P-Blast-phenylphosphate carboxylase subunit delta [Aromatoleum aromaticum]

Xylanase-Xylanases are hydrolytic enzymes which randomly cleave the beta 1,4 backbone of the complex plant cell wall polysaccharide xylan. Diverse forms of these enzymes exist, displaying varying folds, mechanisms of action, substrate specificities, hydrolytic activities (yields, rates and products) and physicochemical characteristics. Research has mainly focused on only two of the xylanase containing glycoside hydrolase families, namely families 10 and 11, yet enzymes with xylanase activity belonging to families 5, 7, 8 and 43 have also been identified and studied, albeit to a lesser extent. Driven by industrial demands for enzymes that can operate under process conditions, a number of extremophilic xylanases have been isolated, in particular those from thermophiles, alkaliphiles and acidiphiles, while little attention has been paid to cold-adapted xylanases. Here, the diverse physicochemical and functional characteristics, as well as the folds and mechanisms of action of all six xylanase containing families will be discussed. The adaptation strategies of the extremophilic xylanases isolated to date and the potential industrial applications of these enzymes will also be presented. P-Blast Xylanase[Filobasidium floriforme]

LaccaseP-Blast laccase [Pinus mugo]

Catechol 1,2-dioxygenaseP-Blast- catechol 1,2-dioxygenase [Acinetobacter baumannii]

Lignin peroxidaseP-Blast-lignin peroxidase [Trametes versicolor]

Manganese peroxidaseP-Blast-manganese peroxidase [Trametes versicolor]

MetaCyc Pathway: phenol degradation I (aerobic):

Summary: Phenols and methyl-substituted phenols can be used by a number of different bacterial and fungal strains including Pseudomonas sp. CF600, which grows efficiently with phenol, cresols, or 3,4-dimethylphenol as the sole carbon and energy source. The most common first step in the aerobic degradation of phenols is hydroxylation to a catechol. In Pseudomonas sp. CF600 this reaction is catalyzed by a multicomponent phenol 2-monooxygenase, encoded by six different gene that are located on pVI150, an IncP-2 megaplasmid [Shingler92, Powlowski94]. These genes are clustered along with 9 other genes that are involved in the catabolism of the catechol to TCA cycle intermediates via a meta-cleavage pathway (see catechol degradation II (meta-cleavage pathway)). Similar operons were found not only on plasmids but also in the chromosomes of some phenol-degrading bacteria such as Pseudomonas putida P35X [Ng94] and Acinetobacter calcoaceticus [Xu03], as well as fungi such as Trichosporon cutaneum [Gerginova]. Phenol 2-monooxygenase: P-Blast: phenol 2-monooxygenase [Sulfobacillus acidophilus DSM 10332]

P-Blast Polyphenol oxidase:

Laccase domain protein yfiH [Escherichia coli PMV-1]

Conserved hypothetical protein E-Coli (243 AA):

NCBI Reference Sequence: YP_008572618.1

hypothetical protein A1A1_18242 [Planococcus antarcticus DSM 14505]

GenBank: EIM05031.1

laccase [Bacillus subtilis]

NCBI Reference Sequence: WP_019714343.1

gi|518544136|ref|WP_019714343. MNTYHPFSLTTPSTLMIQDWIQTNQNNREVIAGFTTKNGGVSQKPFESLN 50 gi|388462627|gb|EIM05031.1| -----------------MKAKLYVNDGQYVSGMTLKDLAEP----ESNN 28 : . . ** * gi|518544136|ref|WP_019714343. TGLHVHDKDADVVKNREYIADMFNIDLQSWVFADQTHDNRVQKVTQRDRG 100 gi|388462627|gb|EIM05031.1| MALHACENPQSVLANRKKLADFISAPVSSFICAQQTHSANFRRVSAKDKG 78 .**. :: .*: **: :**::. ..::*: :*:* gi|518544136|ref|WP_019714343. KGAREYHTALKATDGLYTNEKNVFLALCFADCVPLFFYDPVKSLIGVAHA 150 gi|388462627|gb|EIM05031.1| RGAYDTEDAFSDTDALYTYDSRVVLCSFAADCVPVIIHDRKTGLIGVVHS 128 :** : . *:. **.*** :..*.*. ..****.*: gi|518544136|ref|WP_019714343. GWKGTVKQIGREMVKQWTEQEGSNPSDIYAVIGPSISGACYTVDDRVMDA 200 gi|388462627|gb|EIM05031.1| GWQGTIKEIMSKLLQQLIDLEQCDPVDLDIQIGAAISQQQFEVDQDVYSK 178 **:**:*:* ::::* : * .:* *: : **: * . gi|518544136|ref|WP_019714343. VRALPVSAERAVNQAAQAQYQLDLKELNRLILIDSGLVNEQISVSGLCTE 250 gi|388462627|gb|EIM05031.1| LDSLGYASEFMYFNNMTKKYHIDNQATVKRQCELVGVTSGQIHIDPTCTF 228 : :* ::* : :*::* : ** :. ** gi|518544136|ref|WP_019714343. *: : ::*:* *:

:.*:: *:***.

*****::::*

**.:**

*:..

SEPSLFYSHRRDQGKTGRMMSFIGMKEA 278

gi|388462627|gb|EIM05031.1|

LSLDGFS--YRQDRKSGRHLIFAMKK-- 252 . . * *:: *:** : * *

VSGMTLKDLAEPESNNMALHACENPQSVLANRKKLADFISAPVSSFICAQQTHSANFRRV

SAKDKGRGAYDTEDAFSDTDALYTYDSRVVLCSFAADCVPVIIHDRKTGLIGVVHSGWQG

TIKEIMSKLLQQLIDLEQCDPVDLDIQIGAAISQQQFEVDQDVYSKLDSLGYASEFMYFN

NMTKKYHIDNQATVKRQCELVGVTSGQIHIDPTCTFLSLDGFSYRQDRKSGRHLIF

Pepstats analysis of above sequence:(for amino acid percentage content) PEPSTATS of EMBOSS_001 from 1 to 236 Molecular weight = 26315.70 Residues = 236 Average Residue Weight = 111.507 Charge = -3.5 Isoelectric Point = 5.5698 A280 Molar Extinction Coefficients = 17420 (reduced) 17795 (cystine bridges) A280 Extinction Coefficients 1mg/ml = 0.662 (reduced) 0.676 (cystine bridges) Probability of expression in inclusion bodies = 0.582 Residue A = Ala B = Asx C = Cys D = Asp E = Glu F = Phe G = Gly H = His I = Ile J = --K = Lys L = Leu M = Met N = Asn O = --P = Pro Q = Gln R = Arg S = Ser T = Thr U = --V = Val W = Trp X = Xaa Y = Tyr Z = Glx Property Tiny Small Aliphatic Number 18 0 7 21 9 11 13 7 15 0 13 19 5 8 0 6 16 10 21 12 0 16 1 0 8 0 Residues Number (A+C+G+S+T) (A+B+C+D+G+N+P+S+T+V) (A+I+L+V) Mole% 7.627 0.000 2.966 8.898 3.814 4.661 5.508 2.966 6.356 0.000 5.508 8.051 2.119 3.390 0.000 2.542 6.780 4.237 8.898 5.085 0.000 6.780 0.424 0.000 3.390 0.000 Mole% 71 122 68 30.085 51.695 28.814 DayhoffStat 0.887 0.000 1.023 1.618 0.636 1.295 0.656 1.483 1.412 0.000 0.835 1.088 1.246 0.788 0.000 0.489 1.738 0.865 1.271 0.834 0.000 1.027 0.326 0.000 0.997 0.000

Aromatic Non-polar Polar Charged Basic Acidic

(F+H+W+Y) (A+C+F+G+I+L+M+P+V+W+Y) (D+E+H+K+N+Q+R+S+T+Z) (B+D+E+H+K+R+Z) (H+K+R) (B+D+E+Z)

27 119 117 60 30 30

11.441 50.424 49.576 25.424 12.712 12.712

ProtParam Analysis of above sequence for unstability index:

Number of amino acids: 236 Molecular weight: 26315.7 Theoretical pI: 5.45
CSV format

Amino acid composition: Ala (A) 18 7.6% Arg (R) 10 4.2% Asn (N) 8 3.4% Asp (D) 21 8.9% Cys (C) 7 3.0% Gln (Q) 16 6.8% Glu (E) 9 3.8% Gly (G) 13 5.5% His (H) 7 3.0% Ile (I) 15 6.4% Leu (L) 19 8.1% Lys (K) 13 5.5% Met (M) 5 2.1% Phe (F) 11 4.7% Pro (P) 6 2.5% Ser (S) 21 8.9% Thr (T) 12 5.1% Trp (W) 1 0.4% Tyr (Y) 8 3.4% Val (V) 16 6.8% Pyl (O) 0 0.0% Sec (U) 0 0.0% (B) (Z) (X) 0 0 0 0.0% 0.0% 0.0%

Total number of negatively charged residues (Asp + Glu): 30 Total number of positively charged residues (Arg + Lys): 23 Atomic composition: Carbon Hydrogen Nitrogen Oxygen Sulfur C H N O S 1154 1810 318 362 12

Formula: C1154H1810N318O362S12 Total number of atoms: 3656 Extinction coefficients: Extinction coefficients are in units of water. M-1 cm-1, at 280 nm measured in

Ext. coefficient Abs 0.1% (=1 g/l) Ext. coefficient Abs 0.1% (=1 g/l) Estimated half-life:

17795 0.676, assuming all pairs of Cys residues form cystines 17420 0.662, assuming all Cys residues are reduced

The N-terminal of the sequence considered is V (Val). The estimated half-life is: 100 hours (mammalian reticulocytes, in vitro). >20 hours (yeast, in vivo). >10 hours (Escherichia coli, in vivo). Instability index: The instability index (II) is computed to be 42.84 This classifies the protein as unstable.

Aliphatic index: 83.47 Grand average of hydropathicity (GRAVY): -0.260 Secondary structure elements prediction(NSP@):

Multivariate Linear Regression Combination (SOPMAGOR4-SIMPA) result for : UNK_154910

Abstract Guermeur et al. submitted View MLRC in: [AnTheProt (PC) , Download...] [HELP]
10 20 30 40 50 60 70 | | | | | | | VSGMTLKDLAEPESNNMALHACENPQSVLANRKKLADFISAPVSSFICAQQTHSANFRRVSAKDKGRGAY cccceccccccccccheeeeccccchhhhhhhhhhhhhhccccchhhehhhcccceeeeeeccccccccc DTEDAFSDTDALYTYDSRVVLCSFAADCVPVIIHDRKTGLIGVVHSGWQGTIKEIMSKLLQQLIDLEQCD cccccccccceeeecccceeeeeeccccceeeeeccccceeeeeeccchhhhhhhhhhhhhhhhhhcccc PVDLDIQIGAAISQQQFEVDQDVYSKLDSLGYASEFMYFNNMTKKYHIDNQATVKRQCELVGVTSGQIHI ccceeeeecccccccccccchhhhhhhhhhccccceeecccccccceecchhhhhhhhhhccccccceee DPTCTFLSLDGFSYRQDRKSGRHLIF cccceeccccceeccccccccceecc Sequence length : 236 MLRC : Alpha helix (Hh) : 59 is 25.00% 310 helix (Gg) : 0 is 0.00% Pi helix (Ii) : 0 is 0.00% Beta bridge (Bb) : 0 is 0.00% Extended strand (Ee) : 52 is 22.03% Beta turn (Tt) : 0 is 0.00% Bend region (Ss) : 0 is 0.00% Random coil (Cc) : 125 is 52.97%

Ambigous states (?) Other states

: :

0 is 0 is

0.00% 0.00%

Prediction result file (text): [MLRC] Intermediate result files (text) : [GOR4] [SIMPA96] [SOPMA] View intermediate result files in MPSA : [GOR4] [SIMPA96] [SOPMA] View intermediate result files in ANTHEPROT : [GOR4] [SIMPA96] [SOPMA]
Prediction of Secondary Structural Content from Amino Acid Composition # with Analytic Vector Decomposition # ---------------------------------------------------------------------# Input-Type: Sequence

VSGMTLKDLAEPESNNMALHACENPQSVLANRKKLADFISAPVSSFICAQQTHSANFRRV SAKDKGRGAYDTEDAFSDTDALYTYDSRVVLCSFAADCVPVIIHDRKTGLIGVVHSGWQG TIKEIMSKLLQQLIDLEQCDPVDLDIQIGAAISQQQFEVDQDVYSKLDSLGYASEFMYFN NMTKKYHIDNQATVKRQCELVGVTSGQIHIDPTCTFLSLDGFSYRQDRKSGRHLIF # # # # # # # # # # Thank you for using the WWW-server for SSCP !

1st METHOD The first method relies only on the average amino acid composition of secondary structural segments (helix, sheet, coil) in a learning set of proteins. : 1

method

alpha-contents beta-contents coil-contents class # # # # # # # #

: : : :

33.3 % 26.2 % 40.5 % mixed

2nd METHOD The second method relies also on composition fluctuations in the secondary structural segments (helix, sheet, coil) of a learning set of proteins. : : : : : 2 54.3 % 7.2 % 38.5 % alpha

method alpha-contents beta-contents coil-contents class # #

CLUSTAL W Alignment Multiple Alignment of Phenylphosphate synthase alpha subunit: Sequences from:-

phenylphosphate synthase subunit alpha [Desulfobacula toluolica Tol2] putative phenylphosphate synthase, alpha subunit [Azoarcus sp. KH32C] phenylphosphate synthase, alpha subunit [Geobacter metallireducens GS-15]
putative phenylphosphate synthase alpha subunit PpsA [Clostridia bacterium enrichment culture clone BF]

Phenylphosphate synthase alpha subunit [Aromatoleum aromaticum EbN1] Editing in Box shade:gi|470203970|ref|YP_007598069. 1 YDGLHYPEPLYPFDTIWDEAWYLALSQFNNRIFQVPPVRGVDHRIINGYV 97YISPVPV gi|56313243|emb|CAI07888.1| 1 YDGLHYPEPLYPFDTIWDEAWYLALSQFNNRIFQVPPVRGVDHRIINGYV 97YISPVPV gi|78194562|gb|ABB32329.1| 1 YDGLHYPEPIYPFDTIWDEAWYLGLSQYNNRIFQVPPVRGVDHRIINGYV 95YISPVPV gi|408419048|ref|YP_006760462. 1 NDALHYPEPLYPFDIIWDEAWFLALSQFNTRIFSVPPVYGVDHRIINGNV 98YISPVPV gi|300245771|gb|ADJ93943.1| 1 HDSVHFNPPCTPMGASLNINCMRGSHWAAEWFSLPFSLGFETQVYNGYV 77YHAVNPI gi|470203970|ref|YP_007598069. 58 KDPDEIGRRVPNFMERAGYYYKNWDELEAKWKTKMEGTIAELE gi|56313243|emb|CAI07888.1| 58 KDPAEIGARVPNFMERAGFYYKNWDALEAKWKVKMEAAIAELE gi|78194562|gb|ABB32329.1| 58 TDPEEVGSRVPNFMERAGYYYKNWNELEAKWELKMKGIIKQIE gi|408419048|ref|YP_006760462. 58 TDPEEVQKRIPMFMERAGYYYENWDDLHNQWENKMKGIISEIE gi|300245771|gb|ADJ93943.1| 57

147ALQIPRLPEVEDL 147ALEIPPLPDVEAL 145ELPIPSLPDLEDI 148NLEIASLPDMEDI

TDPAKIEARAVEFGPKLQKALDNWNDFYGEGVQEWSDLLNYLA 127GFQKETLP----gi|470203970|ref|YP_007598069. 114 RVVTDGVGESTAYHLLKNYDDLINLGIRCWQYHFEFL 197NLGYAAYVFFMDFTQKLFP gi|56313243|emb|CAI07888.1| 114 SVVTDGVGESKGYHLLKNYDDLINLGIKCWQYHFEFL 197NLGYAAYVFFMDFTQKLFP gi|78194562|gb|ABB32329.1| 114 SVVTEGIGESKGFHLIKAYDDLINLGIQCWQYHFEFL 195NLGYAAYVFFLDFVQKLFP gi|408419048|ref|YP_006760462. 114 SVVKNGLGTSSGYELLKNYDKLIDLGIRCWQYHFEFL 198NLGYASYVTFVDFCTKAFP gi|300245771|gb|ADJ93943.1| 108 --------FDRLHELLKDAEKTFKR--SWELHFIYM 161YPSFFGYMNFEAICQKYNgi|470203970|ref|YP_007598069. 247AVALEVD-DIVTAHREWADVKAAMA gi|56313243|emb|CAI07888.1| 247AVKLEVD-DIVAGHREWADVKAALA gi|78194562|gb|ABB32329.1| 245AIELGVD-LILTNCGEWQDAETALK gi|408419048|ref|YP_006760462. 248AIELGIDSQIGGDTKDIDDVISELQ gi|300245771|gb|ADJ93943.1| 209AREMGLQ-TVFDVAQKSEDIKGLMK 170 SIPLQRVTQMISGIDVIMYKSDDELKELAKK 170 SIPMQRVTQMISGIDVIMYRPDDELKELAKK 170 SIPLQRVTQMIAGIDVIMYRSDDELKKLAKK 170 DIPLQKVTQMVAGIDVILYRPDDELRKLAKL 152 -INERDMRTFLQGFETKMFEIDREMWHLADL

gi|470203970|ref|YP_007598069. 225 296TGWFHTDRSWNDNLNLPLDGIQTYIGKLRDG gi|56313243|emb|CAI07888.1| 225 296TGWFHTDRSWNDNLDIPLDGIQTYIGKLRAG gi|78194562|gb|ABB32329.1| 225 294TGWSHSDKSWNDDLNIPLSGIATYINQLRQG gi|408419048|ref|YP_006760462. 226 298TGWYHQDVSWNDNLNIPLSSVRIYIGKLNEG gi|300245771|gb|ADJ93943.1| 206 258ALFDMYYKTWNEDPYPVLFTIKTYIQKG--G

GRRHGDEWLAAFEKARYPWFNISSG GHRHGIEWLAAFEKARYPWFNISSG AHPKGRTWLDALEEARYPWFHVSTG GSENGKKWVAAWDEAKYPWFNISTG EKKLGVVWWDQFERFLSKYGKRSTA

gi|470203970|ref|YP_007598069. 281 VAIDRPMEAVRAERDRVTA 346EYRDLIDNDQDRKQFDELLGCARTVFPYVENHLFYVE gi|56313243|emb|CAI07888.1| 281 VSIDRPMEAVRAERERITA 346EYRELIDSDEDRKQFDELLSCAKTVFPYVENHLFYVE gi|78194562|gb|ABB32329.1| 281 MDIERPMEKVRAERDRITE 344EYRDLITSDEDRKTFDELLGTAKTVFPYVENHLFYVE gi|408419048|ref|YP_006760462. 282 KSIDRPLEQIKIERKKLIV 348EYRGLLKTDEDRQTFDQLHGTAELVFPYVENHMFYVE gi|300245771|gb|ADJ93943.1| 260 FDFEEHTKKITDEREKLIE 306ETIARIPAENREEFRIALKHAQDSYPFNEDHNFYVE gi|470203970|ref|YP_007598069. 337 HWFHSVFWNKMRE 396VAAIMQEHGVIAEIEDIWLLRRDEIKQALWDIVTAWATGVTPR gi|56313243|emb|CAI07888.1| 337 HWFHSVFWNKMRE 396VAAIMKEHRMIADIEDIWLLRRDEIKQALWDVVTAWATGVTPR gi|78194562|gb|ABB32329.1| 337 HWFHTVFWRKMRE 394VAAIMKEHGMFEDVEDVWYLRRDEIKQGLWDMVTAWATGVKPR gi|408419048|ref|YP_006760462. 338 HWFHSVFWNKMRA 398VAAIMADNNFLEGQEDIWYMSRSEIKEALWDLVTAWASGTKGY gi|300245771|gb|ADJ93943.1| 315 HWTHCEIRYVILE 355CGRRLVEMGILKEADDVFFLTIGELKGFMEEIIMDERVGIQYF

gi|470203970|ref|YP_007598069. 393 GTKTWPA 446EIEWRKGVMQKFREWAPPPAIGIAPE-VIQEPFTIVLWGVTNSSLSAWA gi|56313243|emb|CAI07888.1| 393 GTATWPA 446EIEWRKGVMQKFREWNPPPAIGVAPE-VIQEPFTIVLWGVTNNSLSDWA gi|78194562|gb|ABB32329.1| 393 GTAVWPK 444EIAWRKGVMKKFQEWSPPPAVGIPPE-VIREPFTIVLWGVTNSSISDWS gi|408419048|ref|YP_006760462. 394 GPLHWPE 448EIQWRKGVYQKFKENIPIPAVGKPPE-TIAEPFTIVLWGITNESMSAWA gi|300245771|gb|ADJ93943.1| 371 GTKVTNT 405VYERKQVWQDMHEFDAPPFIGTIPEHKIEDPVFIKVFGMTDEVIRGSA gi|470203970|ref|YP_007598069. 448 S 495VQEVADPDSITELKGFPASPGTVEGKARVCRSAEEIRDLQEGEILVAPTT gi|56313243|emb|CAI07888.1| 448 A 495VQDIGDPDSITELKGFAASPGTVEGRARVCRSAEDIRDLQEGEILVAPTT gi|78194562|gb|ABB32329.1| 448 E 493VQDISDPDSITTLKGFAGSPGVVEGKARVCRSADDIRLLQEGEILVAPTT gi|408419048|ref|YP_006760462. 449 K 497LKEIGDPDKVNEMEGFAGSPGVAEGIARVCRSVEDIGELKEGEILVAPTT gi|300245771|gb|ADJ93943.1| 426 R 454NTEHVAG---HFEGFPGAPGTVEGVARVVFNYEDFSTVQPDELLVAPFT 500T gi|470203970|ref|YP_007598069. 500 PSWAPAFAKIKACITDVGGVMSHAAIVCREYGMPAVVGTGHS----TRV gi|56313243|emb|CAI07888.1| 500 PSWAPAFAKIKACVTDVGGVMSHAAIVCREYGMPAVVGTGVS----TRV gi|78194562|gb|ABB32329.1| 500 PSWAPAFARIKGAITDVGGVMSHAAIVCREYGMPAVVGTGHA----TKI gi|408419048|ref|YP_006760462. 501 PSWAPVFQKIKAVVTDVGGIMCHAAIVCREYGMPAVVGTGQG----TTI gi|300245771|gb|ADJ93943.1| 474 PAWTPLFSKIRGVVTDSGGMLAHAAICAREYDIPAVVGTITRGVKVTEH

545S 545S 543S 547S

591IKTGMTL 591IRTGMTL 589IRTGMML 593IKSGMKI 550IKTGDRI

gi|470203970|ref|YP_007598069. gi|56313243|emb|CAI07888.1| gi|78194562|gb|ABB32329.1| gi|408419048|ref|YP_006760462. gi|300245771|gb|ADJ93943.1|

552 552 552 553 530

RVDGSSGLVTIVQRVDGSSGVISIITD RVDGATGVVTIDRKVNGDTGKIHIERRIDGTNGKVEIIV-

611 612 609 613 570