ID H7GEA9_9DEIN Unreviewed; 203 AA.
AC H7GEA9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=RLTM_01995 {ECO:0000313|EMBL:EIA40051.1};
OS Thermus parvatiensis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=456163 {ECO:0000313|EMBL:EIA40051.1, ECO:0000313|Proteomes:UP000053186};
RN [1] {ECO:0000313|EMBL:EIA40051.1, ECO:0000313|Proteomes:UP000053186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL {ECO:0000313|EMBL:EIA40051.1,
RC ECO:0000313|Proteomes:UP000053186};
RX PubMed=22689228; DOI=10.1128/JB.00604-12;
RA Dwivedi V., Sangwan N., Nigam A., Garg N., Niharika N., Khurana P.,
RA Khurana J.P., Lal R.;
RT "Draft genome sequence of Thermus sp. strain RL, isolated from a hot water
RT spring located atop the Himalayan ranges at Manikaran, India.";
RL J. Bacteriol. 194:3534-3534(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIA40051.1}.
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DR EMBL; AIJQ01000002; EIA40051.1; -; Genomic_DNA.
DR RefSeq; WP_008631086.1; NZ_AIJQ01000002.1.
DR AlphaFoldDB; H7GEA9; -.
DR PATRIC; fig|456163.3.peg.447; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000053186; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EIA40051.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 3..193
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 203 AA; 21984 MW; FD6804CFA44B12EC CRC64;
MRVKICGITR LQDALLAEAL GAFALGFVFA PGSRRRIAPE AARAIGEALG PFVVRVGVFR
DQPPEEVLRL MEEARLQVAQ LHGEEPPEWA EAVGRFYPVI KAFPLEGPAR PEWADYPAQA
LLLDGKRPGS GEAYPRAWAK PLLATGRRVI LAGGIAPENL EEVLALRPYA LDLASGVEEA
PGVKSAEKLR ALFARLASLR MEG
//
