ID D5BTA1_PUNMI Unreviewed; 217 AA.
AC D5BTA1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272, ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572, ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN OrderedLocusNames=SAR116_1255 {ECO:0000313|EMBL:ADE39498.1};
OS Puniceispirillum marinum (strain IMCC1322).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE39498.1, ECO:0000313|Proteomes:UP000007460};
RN [1] {ECO:0000313|EMBL:ADE39498.1, ECO:0000313|Proteomes:UP000007460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE39498.1,
RC ECO:0000313|Proteomes:UP000007460};
RX PubMed=20382761; DOI=10.1128/JB.00347-10;
RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT IMCC1322, a representative of the SAR116 clade in the
RT Alphaproteobacteria.";
RL J. Bacteriol. 192:3240-3241(2010).
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 -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC Rule:MF_00135}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001751; ADE39498.1; -; Genomic_DNA.
DR RefSeq; WP_013046125.1; NC_014010.1.
DR AlphaFoldDB; D5BTA1; -.
DR STRING; 488538.SAR116_1255; -.
DR KEGG; apb:SAR116_1255; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_1_1_5; -.
DR OrthoDB; 9796196at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000007460; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; Aldolase class I; 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; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
KW Lyase {ECO:0000313|EMBL:ADE39498.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007460};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 6..212
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 217 AA; 23243 MW; EC1C604785F0704B CRC64;
MPRADVKICG IATAADYDVC ARAGARWIGM VFFPKSSRHL SLEVAAALAN HADSYTGDRP
ERVALTVDMA DDALDAVIQA SRPDYIQLHG NETPDRAKAI KARFNVSIIK ALRIGTASDL
DVCSTWDTIA DWLLLDAKSA SSDMPGGTGH SFDWRLLSSY KGMSNWMLAG GLKPDNVTEA
ISMTGARALD VSSGVESALG KKDHGLIRSF IRAAEMG
//
