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MBTI_MYCBO
ID   MBTI_MYCBO              Reviewed;         450 AA.
AC   Q7TYQ1; A0A1R3Y117; X2BKI5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Salicylate synthase {ECO:0000250|UniProtKB:P9WFX1};
DE   AltName: Full=Chorismate mutase {ECO:0000250|UniProtKB:P9WFX1};
DE            Short=CM {ECO:0000250|UniProtKB:P9WFX1};
DE            EC=5.4.99.5 {ECO:0000250|UniProtKB:P9WFX1};
DE   AltName: Full=Isochorismate synthase/isochorismate lyase {ECO:0000250|UniProtKB:P9WFX1};
DE            EC=4.2.99.21 {ECO:0000250|UniProtKB:P9WFX1};
DE            EC=5.4.4.2 {ECO:0000250|UniProtKB:P9WFX1};
DE   AltName: Full=Mycobactin synthase protein {ECO:0000250|UniProtKB:P9WFX1};
GN   Name=mbtI; OrderedLocusNames=BQ2027_MB2407C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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 in a lyase reaction to give
CC       salicylate (isochorismate pyruvate-lyase activity). In the absence of
CC       magnesium, MbtI displays a chorismate mutase activity and converts
CC       chorismate to prephenate. {ECO:0000250|UniProtKB:P9WFX1}.
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:0000250|UniProtKB:P9WFX1};
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:0000250|UniProtKB:P9WFX1};
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:0000250|UniProtKB:P9WFX1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WFX1};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WFX1}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P9WFX1}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       Salicylate synthase subfamily. {ECO:0000250|UniProtKB:P9WFX1}.
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DR   EMBL; LT708304; SIU01019.1; -; Genomic_DNA.
DR   RefSeq; NP_856056.1; NC_002945.3.
DR   RefSeq; WP_003412287.1; NC_002945.4.
DR   AlphaFoldDB; Q7TYQ1; -.
DR   SMR; Q7TYQ1; -.
DR   EnsemblBacteria; SIU01019; SIU01019; BQ2027_MB2407C.
DR   PATRIC; fig|233413.5.peg.2644; -.
DR   OMA; VTDFMTV; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; ISS:UniProtKB.
DR   GO; GO:0043904; F:isochorismate pyruvate lyase activity; ISS:UniProtKB.
DR   GO; GO:0008909; F:isochorismate synthase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009697; P:salicylic acid biosynthetic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Isomerase; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..450
FT                   /note="Salicylate synthase"
FT                   /id="PRO_0000262084"
FT   ACT_SITE        252
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X9I8"
FT   BINDING         270..271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         419..421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         431
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
FT   BINDING         438
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFX1"
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
 
 
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