MBTI_MYCPA
ID MBTI_MYCPA Reviewed; 450 AA.
AC Q73XV3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=MAP_2205c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS04522.1; -; Genomic_DNA.
DR RefSeq; WP_003875926.1; NC_002944.2.
DR AlphaFoldDB; Q73XV3; -.
DR SMR; Q73XV3; -.
DR STRING; 262316.MAP_2205c; -.
DR EnsemblBacteria; AAS04522; AAS04522; MAP_2205c.
DR KEGG; mpa:MAP_2205c; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_2_1_11; -.
DR OMA; VTDFMTV; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000000580; 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; Reference proteome.
FT CHAIN 1..450
FT /note="Salicylate synthase"
FT /id="PRO_0000262085"
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; 48635 MW; 93C76A2A3E1A2E24 CRC64;
MTEVSVETTS AGSESPSIPL PVHIDPADLA AELAVVLSER AGEEYLLYER GGEWVLATGV
RAMIELDSDE LRVIRDGVTQ RQHWSGRPGP VLGEAIDRLL LETDQLFGWI AFEFGVYRYG
LQQRLAPGTA LARVFWPNGR IVVTREAIQL FGTSTGRRDD VLGVLGDGVP GLRDASAVDV
VTDPSNYRDR VASAVAEIAA GRYHKVILSR CLQVPFAVDF PSTYRLARRH NTPVRSFLLR
LGGIRAVGYS PELVAAVRHD GVVVTEPLAG TRAFGRGALH DRQARDDLES NSKEIVEHAI
SVRSSLQEMA EIAEPGTAVV TDFMTVRERG SVQHLGSTVS GRLGTSNDRM DALEALFPAV
TASGIPKAGG VEAILRLDEG PRGLYSGAVV MVSADGALDA ALTLRAAYEH DGKTWLRAGA
GIIEESTPER EFEETCEKLS TLAPYLIARQ
