TRPF_MOOTA
ID TRPF_MOOTA Reviewed; 223 AA.
AC Q2RIT8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; OrderedLocusNames=Moth_1338;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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:0000255|HAMAP-Rule:MF_00135};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
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DR EMBL; CP000232; ABC19651.1; -; Genomic_DNA.
DR RefSeq; WP_011392851.1; NC_007644.1.
DR RefSeq; YP_430194.1; NC_007644.1.
DR AlphaFoldDB; Q2RIT8; -.
DR SMR; Q2RIT8; -.
DR STRING; 264732.Moth_1338; -.
DR EnsemblBacteria; ABC19651; ABC19651; Moth_1338.
DR KEGG; mta:Moth_1338; -.
DR PATRIC; fig|264732.11.peg.1436; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_9; -.
DR OMA; FYAKSPR; -.
DR UniPathway; UPA00035; UER00042.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW Tryptophan biosynthesis.
FT CHAIN 1..223
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000018610"
SQ SEQUENCE 223 AA; 24112 MW; 25067EEA29065F07 CRC64;
MVRVKICGIR DWEEARMVLD AGVDTLGFVF ARSPRAIKPE AAREIITKLP PFTTTVGVFV
NEPRYSLMEI ASFCRLDVLQ LHGDEPPEYC HGLSQRLIKA IRVRDAASLA SLEAYREVQG
FLLDAWVPGK AGGTGTTFNW ELVRGAATGG KPVILAGGLT PENVGAAIQL VHPYAVDVSS
GVEVDGRKNP ARIAAFLEAV RKAEEHHVRP TASSCCTGLK GDF