MBTI_MYCTO
ID MBTI_MYCTO Reviewed; 450 AA.
AC P9WFX0; 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 36.
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; Synonyms=trpE2; OrderedLocusNames=MT2454;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK46749.1; -; Genomic_DNA.
DR RefSeq; WP_003412287.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WFX0; -.
DR SMR; P9WFX0; -.
DR BindingDB; P9WFX0; -.
DR EnsemblBacteria; AAK46749; AAK46749; MT2454.
DR KEGG; mtc:MT2454; -.
DR PATRIC; fig|83331.31.peg.2645; -.
DR HOGENOM; CLU_006493_2_1_11; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001020; 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_0000428463"
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
