TRPF_BREBN
ID TRPF_BREBN Reviewed; 222 AA.
AC C0ZCE4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=BBR47_24760;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH43453.1; -; Genomic_DNA.
DR RefSeq; WP_012686160.1; NC_012491.1.
DR AlphaFoldDB; C0ZCE4; -.
DR SMR; C0ZCE4; -.
DR STRING; 358681.BBR47_24760; -.
DR EnsemblBacteria; BAH43453; BAH43453; BBR47_24760.
DR KEGG; bbe:BBR47_24760; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_1_0_9; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001877; Chromosome.
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 Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..222
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000197084"
SQ SEQUENCE 222 AA; 23758 MW; F546C9DB7B1A33C4 CRC64;
MTRLKICGIK RTETLALLKE LEVDYVGLVF APSKRQVDAQ TAGQLLAAVP GHPPAVGVFV
NPTMEELEEV LSEAPLSVIQ LHGQETPQFC QQVRERFALP VWKALAVGGE ADAALAIQSY
QGIVSAFLFD TYDPGQAGGT GKKFSWEQIP ALQAACEAAD CIIAGGIHAE NVGELMGQYQ
AGIVDVSSGV ETDGVKDAQK IKTLVERVKA HEQHSNNYAS RA