ID D2Z6G2_9BACT Unreviewed; 207 AA.
AC D2Z6G2;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=Dpep_1033 {ECO:0000313|EMBL:EFC91059.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91059.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC91059.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91059.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
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:EFC91059.1}.
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DR EMBL; ABTR02000001; EFC91059.1; -; Genomic_DNA.
DR RefSeq; WP_005660214.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z6G2; -.
DR STRING; 469381.Dpep_1033; -.
DR PaxDb; 469381-Dpep_1033; -.
DR eggNOG; COG0135; Bacteria.
DR OrthoDB; 9786954at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000006427; 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:EFC91059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 3..197
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 207 AA; 22095 MW; 45CD6DC341F98B9A CRC64;
MKIKICGLTR REDVETALSL GVDALGFILA DSPRKVSLED VSSLVEGLPP FSSTVAVVAN
PSDSDLREIV SSRLFDCVQF HGSESPEIVA SVPIRTIKAF GIASKEDLDE ALSYGGGDWL
LLDGRVGRAT GGTGRPFDWK ILRGRQIGRP WILAGGLGPD NLEKAVWTTT PPAVDLNSAL
ETAPGIKDGN RMARAVEIVR GLEGEEL
//
