GenomeNet

Database: UniProt
Entry: A0A0Q9A537_9FLAO
LinkDB: A0A0Q9A537_9FLAO
Original site: A0A0Q9A537_9FLAO 
ID   A0A0Q9A537_9FLAO        Unreviewed;       210 AA.
AC   A0A0Q9A537;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=ASE21_02445 {ECO:0000313|EMBL:KRD12788.1};
OS   Flavobacterium sp. Root901.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD12788.1, ECO:0000313|Proteomes:UP000051400};
RN   [1] {ECO:0000313|EMBL:KRD12788.1, ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|EMBL:KRD12788.1,
RC   ECO:0000313|Proteomes:UP000051400};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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|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:KRD12788.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMJB01000001; KRD12788.1; -; Genomic_DNA.
DR   RefSeq; WP_057120972.1; NZ_LMJB01000001.1.
DR   AlphaFoldDB; A0A0Q9A537; -.
DR   STRING; 1736605.ASE21_02445; -.
DR   OrthoDB; 9786954at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000051400; 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:KRD12788.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          4..201
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
SQ   SEQUENCE   210 AA;  24070 MW;  EA2E5FA4F88BE9F9 CRC64;
     MKLKICGMKY PENILEVGAL LPDYMGFIFW EKSARYFNGT IPELIKTIKK VGVFVDQSQE
     EILEKVTKYN LQAVQLHGNE TVEFCAELKS KLSKKIEIIK AFSANENFDF EVIKPFEEVS
     DYFLFDTKGK LPGGNGTTFD WTILKKYNSE KPFFLSGGIG INELKAIEEI SKSNLPIYAI
     DVNSKFEIEP GLKNRNLFSN FKRKFDVANF
//
DBGET integrated database retrieval system