ID A0A0M4CFT4_9CORY Unreviewed; 474 AA.
AC A0A0M4CFT4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpC {ECO:0000313|EMBL:ALC07078.1};
GN Synonyms=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=CDES_13755 {ECO:0000313|EMBL:ALC07078.1};
OS Corynebacterium deserti GIMN1.010.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=931089 {ECO:0000313|EMBL:ALC07078.1, ECO:0000313|Proteomes:UP000068067};
RN [1] {ECO:0000313|EMBL:ALC07078.1, ECO:0000313|Proteomes:UP000068067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMN1.010 {ECO:0000313|EMBL:ALC07078.1,
RC ECO:0000313|Proteomes:UP000068067};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium deserti GIMN1.010 (=DSM
RT 45689), isolated from desert sand in western China.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025592}.
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 Evidence={ECO:0000256|ARBA:ARBA00001633};
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; Evidence={ECO:0000256|ARBA:ARBA00001164,
CC ECO:0000256|HAMAP-Rule:MF_00135};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC Rule:MF_00135}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC {ECO:0000256|ARBA:ARBA00009847}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC {ECO:0000256|ARBA:ARBA00007902}.
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DR EMBL; CP009220; ALC07078.1; -; Genomic_DNA.
DR RefSeq; WP_053545943.1; NZ_CP009220.1.
DR AlphaFoldDB; A0A0M4CFT4; -.
DR STRING; 931089.CDES_13755; -.
DR KEGG; cdx:CDES_13755; -.
DR PATRIC; fig|931089.4.peg.2780; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000068067; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
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; Aldolase class I; 2.
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:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00135};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00135};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ALC07078.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00135}.
FT DOMAIN 10..258
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 263..449
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 474 AA; 50439 MW; E12F4FD57CD18887 CRC64;
MTSNNLPTVL EGIVEGRRGH LKEIRARIAH VDVDALPKST RSLFDSLNHG RGNARFIMEC
KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG GDYDHLATVA ATTHLPVLCK
DFIIDPVQIH AARYFGADAV LLMLSVLDDA EYAALSAEAA RFDLDVLTEV IDEEEVERAI
KLGAKIFGVN HRNLHDLSID LDRSGRLAQL IPTDAVLISE SGVRNTETVR QLGGHSNGFL
VGSQLTSQPN VDIAARELVY GPNKVCGLTS ETAAQAARAA GAVYGGFIFE EASPRNVSRE
TSQKIIAAEP SLRYVAVSRR TSGYQELLVD GITAVQIHAP LQGSVEAEQA LVAAVRAEVG
DQVEVWRAVS MSSALGAEVA VALADSVDKL VLDAHEGGSG QPFDWSTIPA EVKAKSLLAG
GLNPDNITDA LAVGCAGLDI NSGVEYPAGA GEWAGAKDSG ALLKIFATIS TFHY
//
