ID S0AP53_FERAC Unreviewed; 199 AA.
AC S0AP53;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=FACI_IFERC00001G1078 {ECO:0000313|EMBL:AGO61058.1};
OS Ferroplasma acidarmanus Fer1.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Ferroplasmaceae; Ferroplasma.
OX NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO61058.1, ECO:0000313|Proteomes:UP000014660};
RN [1] {ECO:0000313|EMBL:AGO61058.1, ECO:0000313|Proteomes:UP000014660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA Banfield J.F.;
RT "Genome dynamics in a natural archaeal population.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(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: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|ARBA:ARBA00007571,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
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DR EMBL; CP004145; AGO61058.1; -; Genomic_DNA.
DR RefSeq; WP_009887111.1; NC_021592.1.
DR AlphaFoldDB; S0AP53; -.
DR GeneID; 16025248; -.
DR KEGG; fac:FACI_IFERC01G1078; -.
DR HOGENOM; CLU_076364_3_0_2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000014660; 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; 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:AGO61058.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014660};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 3..187
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 199 AA; 22314 MW; C39D31BD1D250628 CRC64;
MKVKVCGITR IEDAEYAIKM GADLIGVILD PEVGRHGSQA LIREIKTKYP STPIAGVYTS
MPEHAGYEDY IQLHFNHSGE DIIAAKKAFN KKIISVVDFH EEGIADKVDS HMKSGAEIIL
LEDRSGIINR IDQVKELPRE RLGIAGKIDS NNVQKLLATE PYLVDVSSSL EEYTGKKSFK
KIDEFFNKIG EYYAVRQNQ
//
