ID M1Y158_NATM8 Unreviewed; 208 AA.
AC M1Y158;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ECO:0000313|EMBL:CCQ36227.1};
GN OrderedLocusNames=Nmlp_2043 {ECO:0000313|EMBL:CCQ36227.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ36227.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ36227.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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; HF582854; CCQ36227.1; -; Genomic_DNA.
DR RefSeq; WP_015409032.1; NC_020388.1.
DR AlphaFoldDB; M1Y158; -.
DR STRING; 268739.Nmlp_2043; -.
DR GeneID; 14653293; -.
DR KEGG; nmo:Nmlp_2043; -.
DR eggNOG; arCOG01983; Archaea.
DR HOGENOM; CLU_076364_2_1_2; -.
DR OrthoDB; 27513at2157; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000011867; 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:CCQ36227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 4..202
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 208 AA; 21109 MW; D2A033308AD8C82A CRC64;
MTRVKICGVT TREDLGAVVE AGADAIGVTV DVPVETPRAI DAERAADIVS ATPPFVTTVL
VTMPDPPASA AGVAERVGAD VVQLHGDLPP EGVASLSADL ESDVVVAVSP DDAPRYDTVA
DALLVDSLDE SGAGGTGATH DWERTRELVS ELASPVVLAG GLTPENVAKA VETVDPFAVD
VASGVEGQPG RKDPAALEAF VRRAGGRP
//
