ID A0A0S3QVC1_THET7 Unreviewed; 185 AA.
AC A0A0S3QVC1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ECO:0000313|EMBL:BAT72276.1};
GN ORFNames=TST_1490 {ECO:0000313|EMBL:BAT72276.1};
OS Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS ABI70S6).
OC Bacteria; Aquificota; Aquificae; Aquificales.
OX NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT72276.1, ECO:0000313|Proteomes:UP000063234};
RN [1] {ECO:0000313|Proteomes:UP000063234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6
RC {ECO:0000313|Proteomes:UP000063234};
RX PubMed=29420286; DOI=10.1126/science.aao3407;
RA Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA Fujita N., Takaki Y., Atomi H., Takai K.;
RT "A primordial and reversible TCA cycle in a facultatively
RT chemolithoautotrophic thermophile.";
RL Science 359:559-563(2018).
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}.
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DR EMBL; AP013035; BAT72276.1; -; Genomic_DNA.
DR RefSeq; WP_070098528.1; NZ_AP013035.1.
DR AlphaFoldDB; A0A0S3QVC1; -.
DR STRING; 1298851.TST_1490; -.
DR KEGG; ttk:TST_1490; -.
DR PATRIC; fig|1298851.3.peg.1565; -.
DR OrthoDB; 9786954at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000063234; 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; Aldolase class I; 2.
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, ECO:0000313|EMBL:BAT72276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063234};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 101..178
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 185 AA; 20482 MW; BBE6179AB35395CB CRC64;
MVFVKICGIR DVDTALVAVR AGADAIGLVF HRESPRFVGI ELAKEIGEAV KGKVKVFAVI
KNSNEFDERF FDVCDYVQCY EPIPGLDSSK LVLGVKGFTD YKAAYYIVDA SHGKGMFVEY
PHDLWRLPKD RVILSGGLTP DNVKEVIRKY RPFGVDVSSG VEVSPGVKDP EKVVQFVRNA
KEALP
//
