TRPF_SULNB
ID TRPF_SULNB Reviewed; 196 AA.
AC A6QC86;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=SUN_2155;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF73095.1; -; Genomic_DNA.
DR RefSeq; WP_012083925.1; NC_009663.1.
DR AlphaFoldDB; A6QC86; -.
DR SMR; A6QC86; -.
DR STRING; 387093.SUN_2155; -.
DR EnsemblBacteria; BAF73095; BAF73095; SUN_2155.
DR KEGG; sun:SUN_2155; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_7; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000006378; 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..196
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000197130"
SQ SEQUENCE 196 AA; 21967 MW; 401EEB1FD61B918B CRC64;
MRVKICGITN LRDALHAVEC GADALGFVFY NESPRYITPK DAKRIIDQLP PFVERVGLFV
NEGVETIDTV CRYSDISLAQ IHFDVDEESL DAISLKTLPV VRARTAEDVH RFPDRYRLVD
AYCEAYGGSG KRLNLEWFDG VDCSRIILAG GLTPDNVNEV KQYGFYGVDV SSGVESVKGK
KDLQKVERFL RNAKSL