TRPC_VIBPA
ID TRPC_VIBPA Reviewed; 481 AA.
AC P22098;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 25-MAY-2022, entry version 135.
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; Synonyms=trpC-TRPF; OrderedLocusNames=VP1959;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RX PubMed=1773058; DOI=10.3109/10425179109020770;
RA Crawford I.P., Han C.Y., Silverman M.;
RT "Sequence and features of the tryptophan operon of Vibrio
RT parahemolyticus.";
RL DNA Seq. 1:189-196(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; X17149; CAA35034.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC60222.1; -; Genomic_DNA.
DR RefSeq; NP_798338.1; NC_004603.1.
DR AlphaFoldDB; P22098; -.
DR SMR; P22098; -.
DR STRING; 223926.28806951; -.
DR EnsemblBacteria; BAC60222; BAC60222; BAC60222.
DR KEGG; vpa:VP1959; -.
DR PATRIC; fig|223926.6.peg.1874; -.
DR eggNOG; COG0134; Bacteria.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_007713_1_1_6; -.
DR OMA; YDIIGIN; -.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000002493; Chromosome 1.
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..481
FT /note="Tryptophan biosynthesis protein TrpCF"
FT /id="PRO_0000154286"
FT REGION 1..283
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 284..481
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT CONFLICT 203
FT /note="R -> K (in Ref. 1; CAA35034)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="G -> A (in Ref. 1; CAA35034)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="H -> R (in Ref. 1; CAA35034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52974 MW; BC575AD8FB57FC00 CRC64;
MKMTDFNTQQ ANNLSEHVSK KEAEMAEVLA KIVRDKYQWV AERKASQHLS TFQSDLLPSD
RSFYDALSGD KTVFITECKK ASPSKGLIRN DFDLDYIASV YNNYADAISV LTDEKYFQGS
FDFLPQVRRQ VKQPVLCKDF MVDTYQVYLA RHYGADAVLL MLSVLNDEEY KALEEAAHSL
NMGILTEVSN EEELHRAVQL GARVIGINNR NLRDLTTDLN RTKALAPTIR KLAPNATVIS
ESGIYTHQQV RDLAEYADGF LIGSSLMAED NLELAVRKVT LGENKVCGLT HPDDAAKAYQ
AGAVFGGLIF VEKSKRAVDF ESARLTMSGA PLNYVGVFQN HDVDYVASIV TSLGLKAVQL
HGLEDQEYVN QLKTELPVGV EIWKAYGVAD TKPSLLADNI DRHLLDAQVG TQTGGTGHVF
DWSLIGDPSQ IMLAGGLSPE NAQQAAKLGC LGLDLNSGVE SAPGKKDSQK LQAAFHAIRN
Y
