ID A0A0P0N3K5_9CREN Unreviewed; 220 AA.
AC A0A0P0N3K5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=Pyrde_0936 {ECO:0000313|EMBL:ALL00984.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL00984.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL00984.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL00984.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013011; ALL00984.1; -; Genomic_DNA.
DR RefSeq; WP_055410739.1; NZ_NCQP01000001.1.
DR AlphaFoldDB; A0A0P0N3K5; -.
DR STRING; 1273541.Pyrde_0936; -.
DR GeneID; 26099275; -.
DR KEGG; pdl:Pyrde_0936; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000058613; 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:ALL00984.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 7..214
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 220 AA; 23794 MW; FE52820815E3200A CRC64;
MLRPKLKICG LTRRDDVEAL DGLADYLGFI VAREKVSPRV LEPSKARDLV ETVAKSRRVL
VAHGYTPHEA LDLAARLEVF HVLQYHQPAN PGELESLATG LEELGMGLAP VSLWNGERLA
PDPCSVAQAV PVHEYLLVDA LKTLKKRYRA GLRVPLDAYC RAVSCTERAA AAGGIDPGNV
CLAASTGVYM IDVSSGVEAE PGRKDLEKVK QLIEVLGQCS
//
