MBTI_MYCTU
ID MBTI_MYCTU Reviewed; 450 AA.
AC P9WFX1; L0T9G8; Q79FE7; Q7D785;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Salicylate synthase {ECO:0000303|PubMed:16923875};
DE AltName: Full=Chorismate mutase {ECO:0000303|PubMed:17240979};
DE Short=CM {ECO:0000303|PubMed:17240979};
DE EC=5.4.99.5 {ECO:0000269|PubMed:17240979};
DE AltName: Full=Isochorismate synthase/isochorismate lyase {ECO:0000303|PubMed:9831524};
DE EC=4.2.99.21 {ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979, ECO:0000269|PubMed:20512795};
DE EC=5.4.4.2 {ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979, ECO:0000269|PubMed:20512795};
DE AltName: Full=Mycobactin synthase protein {ECO:0000305|PubMed:9831524};
GN Name=mbtI {ECO:0000303|PubMed:9831524};
GN Synonyms=trpE2 {ECO:0000303|PubMed:9831524}; OrderedLocusNames=Rv2386c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=9831524; DOI=10.1016/s1074-5521(98)90291-5;
RA Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.;
RT "Identification of a Mycobacterium tuberculosis gene cluster encoding the
RT biosynthetic enzymes for assembly of the virulence-conferring siderophore
RT mycobactin.";
RL Chem. Biol. 5:631-645(1998).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11722747; DOI=10.1046/j.1365-2958.2001.02684.x;
RA Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I.;
RT "The Mycobacterium tuberculosis IdeR is a dual functional regulator that
RT controls transcription of genes involved in iron acquisition, iron storage
RT and survival in macrophages.";
RL Mol. Microbiol. 42:851-865(2001).
RN [4]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=16508110; DOI=10.1107/s1744309104031215;
RA Harrison A.J., Ramsay R.J., Baker E.N., Lott J.S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of MbtI, a
RT protein essential for siderophore biosynthesis in Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. F 61:121-123(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20487026; DOI=10.1111/j.1574-6968.2010.02004.x;
RA Nagachar N., Ratledge C.;
RT "Roles of trpE2, entC and entD in salicylic acid biosynthesis in
RT Mycobacterium smegmatis.";
RL FEMS Microbiol. Lett. 308:159-165(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16923875; DOI=10.1128/jb.00338-06;
RA Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J.,
RA Baker E.N., Lott J.S.;
RT "The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in
RT the biosynthesis of the siderophore mycobactin, reveals it to be a
RT salicylate synthase.";
RL J. Bacteriol. 188:6081-6091(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=17240979; DOI=10.1021/bi060852x;
RA Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.;
RT "Structure and mechanism of MbtI, the salicylate synthase from
RT Mycobacterium tuberculosis.";
RL Biochemistry 46:954-964(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=20512795; DOI=10.1002/cmdc.201000137;
RA Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S.,
RA Payne R.J.;
RT "Inhibition studies of Mycobacterium tuberculosis salicylate synthase
RT (MbtI).";
RL ChemMedChem 5:1067-1079(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=22607697; DOI=10.1021/bi3002067;
RA Chi G., Manos-Turvey A., O'Connor P.D., Johnston J.M., Evans G.L.,
RA Baker E.N., Payne R.J., Lott J.S., Bulloch E.M.;
RT "Implications of binding mode and active site flexibility for inhibitor
RT potency against the salicylate synthase from Mycobacterium tuberculosis.";
RL Biochemistry 51:4868-4879(2012).
CC -!- FUNCTION: Involved in the incorporation of salicylate into the
CC virulence-conferring salicylate-based siderophore mycobactin. Catalyzes
CC the initial conversion of chorismate to yield the intermediate
CC isochorismate (isochorismate synthase activity), and the subsequent
CC elimination of the enolpyruvyl side chain to give salicylate
CC (isochorismate pyruvate-lyase activity). In the absence of magnesium,
CC MbtI displays a chorismate mutase activity and converts chorismate to
CC prephenate. {ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979,
CC ECO:0000269|PubMed:20487026, ECO:0000269|PubMed:20512795,
CC ECO:0000269|PubMed:9831524}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC Evidence={ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979,
CC ECO:0000269|PubMed:20512795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isochorismate = pyruvate + salicylate; Xref=Rhea:RHEA:27874,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:29780, ChEBI:CHEBI:30762;
CC EC=4.2.99.21; Evidence={ECO:0000269|PubMed:16923875,
CC ECO:0000269|PubMed:17240979, ECO:0000269|PubMed:20512795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000269|PubMed:17240979};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979,
CC ECO:0000269|PubMed:20512795};
CC -!- ACTIVITY REGULATION: Inhibited by (E)-3-(1-carboxyprop-1-enyloxy)-2-
CC hydroxybenzoic acid (AMT), 3-(1-carboxy-2-phenylvinyloxy)-2-
CC hydroxybenzoic acid (phenyl-AMT), 3-(1-carboxy-3-methylbut-1-enyloxy)-
CC 2-hydroxybenzoic acid, 3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid
CC (ethyl-AMT), 3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid (methyl-
CC AMT), 3-(1-carboxy-2-cyclopropylethenyloxy)-2-hydroxybenzoic acid
CC (cyclopropyl-AMT) and 3-(1-carboxy-3-methylbut-1-enyloxy)-2-
CC hydroxybenzoic acid (isopropyl-AMT). {ECO:0000269|PubMed:20512795,
CC ECO:0000269|PubMed:22607697}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for isochorismate (for isochorismate pyruvate lyase
CC activity at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17240979};
CC KM=6 uM for isochorismate (for salicylate synthase activity at pH 8
CC and 37 degrees Celsius) {ECO:0000269|PubMed:17240979};
CC KM=21 uM for isochorismate (for salicylate synthase activity at pH 8
CC and 25 degrees Celsius) {ECO:0000269|PubMed:20512795};
CC KM=26 uM for chorismate (for chorismate mutase activity without
CC magnesium at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17240979};
CC KM=34 uM for chorismate (for isochorismate synthase activity at pH 7
CC and 37 degrees Celsius) {ECO:0000269|PubMed:17240979};
CC Note=kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity
CC (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate
CC synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-
CC 1) for isochorismate synthase activity (at pH 7 and 37 degrees
CC Celsius). kcat is 4.5 min(-1) for chorismate mutase activity (without
CC magnesium at pH 7.5 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:17240979};
CC pH dependence:
CC At pH below 7.5, MtbI produces isochorismate and at pH 8 it produces
CC salicylate. {ECO:0000269|PubMed:17240979};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC {ECO:0000305|PubMed:9831524}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16508110,
CC ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:17240979,
CC ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697}.
CC -!- INDUCTION: Induced by iron starvation conditions and during infection
CC of human THP-1 macrophages. Transcriptionally repressed by IdeR and
CC iron. {ECO:0000269|PubMed:11722747}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a reduction in
CC salicylic acid biosynthesis and a drastic decrease in production of
CC mycobactin compared with the wild-type strain.
CC {ECO:0000269|PubMed:20487026}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC Salicylate synthase subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP45174.1; -; Genomic_DNA.
DR RefSeq; WP_003412287.1; NZ_NVQJ01000029.1.
DR RefSeq; YP_177877.1; NC_000962.3.
DR PDB; 2G5F; X-ray; 1.80 A; A/B/C/D=2-450.
DR PDB; 2I6Y; X-ray; 2.50 A; A=2-450.
DR PDB; 3LOG; X-ray; 1.73 A; A/B/C/D=1-449.
DR PDB; 3RV6; X-ray; 2.04 A; A/B=2-450.
DR PDB; 3RV7; X-ray; 2.50 A; A/B/C/D=2-450.
DR PDB; 3RV8; X-ray; 2.29 A; A/B/C/D=1-450.
DR PDB; 3RV9; X-ray; 2.14 A; A/B/C/D=2-450.
DR PDB; 3ST6; X-ray; 1.75 A; A/B/C/D=1-450.
DR PDB; 3VEH; X-ray; 2.00 A; A/B/C/D=1-449.
DR PDB; 6ZA4; X-ray; 2.09 A; A/B/C/D=1-450.
DR PDB; 6ZA5; X-ray; 2.11 A; A/B/C/D=1-450.
DR PDB; 6ZA6; X-ray; 1.80 A; A/B/C/D=1-450.
DR PDBsum; 2G5F; -.
DR PDBsum; 2I6Y; -.
DR PDBsum; 3LOG; -.
DR PDBsum; 3RV6; -.
DR PDBsum; 3RV7; -.
DR PDBsum; 3RV8; -.
DR PDBsum; 3RV9; -.
DR PDBsum; 3ST6; -.
DR PDBsum; 3VEH; -.
DR PDBsum; 6ZA4; -.
DR PDBsum; 6ZA5; -.
DR PDBsum; 6ZA6; -.
DR AlphaFoldDB; P9WFX1; -.
DR SMR; P9WFX1; -.
DR STRING; 83332.Rv2386c; -.
DR SwissLipids; SLP:000001285; -.
DR PaxDb; P9WFX1; -.
DR DNASU; 885823; -.
DR GeneID; 885823; -.
DR KEGG; mtu:Rv2386c; -.
DR TubercuList; Rv2386c; -.
DR eggNOG; COG1169; Bacteria.
DR OMA; VTDFMTV; -.
DR PhylomeDB; P9WFX1; -.
DR BRENDA; 4.2.99.21; 3445.
DR BRENDA; 5.4.4.2; 3445.
DR UniPathway; UPA00011; -.
DR PRO; PR:P9WFX1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:MTBBASE.
DR GO; GO:0043904; F:isochorismate pyruvate lyase activity; IDA:MTBBASE.
DR GO; GO:0008909; F:isochorismate synthase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; IDA:MTBBASE.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:MTBBASE.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR019996; Salicylate_synthase.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR03494; salicyl_syn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..450
FT /note="Salicylate synthase"
FT /id="PRO_0000262086"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9X9I8"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20512795,
FT ECO:0000269|PubMed:22607697"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20512795"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16923875,
FT ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16923875,
FT ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697"
FT BINDING 419..421
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16923875,
FT ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20512795"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20512795"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16923875,
FT ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697"
FT SITE 268
FT /note="Could activate a water molecule for attack at the C2
FT of chorismate and involved in recognition/elimination of
FT the C4 hydroxyl"
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 205
FT /note="K->A: Only the chorismate mutase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 252
FT /note="E->Q: No activity is observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 268
FT /note="L->A: Only the chorismate mutase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 271
FT /note="T->A: Only the chorismate mutase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 334
FT /note="H->M: Only the chorismate mutase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT MUTAGEN 405
FT /note="R->A: Only the chorismate mutase activity is
FT observed."
FT /evidence="ECO:0000269|PubMed:17240979"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:3LOG"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 53..67
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 292..310
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 319..329
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 332..343
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:3LOG"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3LOG"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:3LOG"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3LOG"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:3LOG"
SQ SEQUENCE 450 AA; 48754 MW; 79D95307E025D28A CRC64;
MSELSVATGA VSTASSSIPM PAGVNPADLA AELAAVVTES VDEDYLLYEC DGQWVLAAGV
QAMVELDSDE LRVIRDGVTR RQQWSGRPGA ALGEAVDRLL LETDQAFGWV AFEFGVHRYG
LQQRLAPHTP LARVFSPRTR IMVSEKEIRL FDAGIRHREA IDRLLATGVR EVPQSRSVDV
SDDPSGFRRR VAVAVDEIAA GRYHKVILSR CVEVPFAIDF PLTYRLGRRH NTPVRSFLLQ
LGGIRALGYS PELVTAVRAD GVVITEPLAG TRALGRGPAI DRLARDDLES NSKEIVEHAI
SVRSSLEEIT DIAEPGSAAV IDFMTVRERG SVQHLGSTIR ARLDPSSDRM AALEALFPAV
TASGIPKAAG VEAIFRLDEC PRGLYSGAVV MLSADGGLDA ALTLRAAYQV GGRTWLRAGA
GIIEESEPER EFEETCEKLS TLTPYLVARQ
