ID   TRPC_PASMU              Reviewed;         469 AA.
AC   P57855;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Tryptophan biosynthesis protein TrpCF;
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase;
DE              Short=IGPS;
DE              EC=4.1.1.48;
DE   Includes:
DE     RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase;
DE              Short=PRAI;
DE              EC=5.3.1.24;
GN   Name=trpC; OrderedLocusNames=PM0580;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC       tryptophan biosynthetic pathway. The first reaction is catalyzed by the
CC       isomerase, coded by the TrpF domain; the second reaction is catalyzed
CC       by the synthase, coded by the TrpC domain (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC         carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC         EC=5.3.1.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC       {ECO:0000305}.
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DR   EMBL; AE004439; AAK02664.1; -; Genomic_DNA.
DR   RefSeq; WP_010906737.1; NC_002663.1.
DR   AlphaFoldDB; P57855; -.
DR   SMR; P57855; -.
DR   STRING; 747.DR93_1359; -.
DR   EnsemblBacteria; AAK02664; AAK02664; PM0580.
DR   KEGG; pmu:PM0580; -.
DR   PATRIC; fig|272843.6.peg.587; -.
DR   HOGENOM; CLU_007713_1_2_6; -.
DR   OMA; YDIIGIN; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00331; IGPS; 1.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 2.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Isomerase; Lyase; Multifunctional enzyme; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..469
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154282"
FT   REGION          1..267
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          268..469
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   469 AA;  52851 MW;  CD1FD2866ADF10C8 CRC64;
     MTQAFPSILQ KIIQDKTTWI AEKQAQLPLA SFQDQLERSD RDFYQAMQQG SKQRPSYILE
     CKKASPSKGL IRAAFDLTEI AEVYQHYATV ISVLTDEKYF QGHFADIAQV RQRVTQPILC
     KDFILSEYQV YLARYAQADA ILLMLSVLND ERYTQLATLA HQLGMGVLTE TSNEAEFARA
     LALKAKVIGV NNRNLHDLSV DIQRVAQITQ HYADQIPPET KIISESGIYQ HQQIRDLRHV
     ADGFLIGSSL MQHTDLNHAV RSLLFGEHKV CGLTRPQDVR AVYQQGALYG GLIFVTHSKR
     CISLRQAQEL VTQAPLRFVG VFQDQSIAFI CHLATQLRLH AVQLHGNESH EFIRQLRDEL
     PVNCEIWRAI CIESSGTSPC QIVENKNIDR YIFDSKTHQQ RGGTGKTFDW QLIPHHLKPK
     SMLAGGITPE NIPLALAQGC LGLDLNSGLE TYPGVKSHQK VVAAFAQLR