TRPF_BRUA2
ID TRPF_BRUA2 Reviewed; 222 AA.
AC Q2YQW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-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=BAB1_2113;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ12069.1; -; Genomic_DNA.
DR RefSeq; WP_002965175.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YQW4; -.
DR SMR; Q2YQW4; -.
DR STRING; 359391.BAB1_2113; -.
DR EnsemblBacteria; CAJ12069; CAJ12069; BAB1_2113.
DR GeneID; 45053036; -.
DR GeneID; 55591677; -.
DR KEGG; bmf:BAB1_2113; -.
DR PATRIC; fig|359391.11.peg.1344; -.
DR HOGENOM; CLU_076364_1_1_5; -.
DR OMA; FYAKSPR; -.
DR PhylomeDB; Q2YQW4; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000002719; Chromosome I.
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_1000018585"
SQ SEQUENCE 222 AA; 23614 MW; 28E7AFA3258F5514 CRC64;
MALDIKICGL KTPEAVAAAL DGGATHIGFI FFPKSPRHIT PDAAARLRAA ATGRAVAVAV
TVDADDEALD EIVKTVRPDM LQLHGGETPE RVRFLKERYN LPVMKAFSIR EAGDLEAIAP
YRGIADRFLF DAKPPKGSEL PGGNGISFDW NLLAALDADI DYMLSGGLNA DNIAEALLKT
GAPGIDISSG VECAPGEKDV RLIENFFQAV ADANAQPFAR RA