(data stored in SCRATCH zone)

SWISSPROT: A4AT93_MARSH

ID   A4AT93_MARSH            Unreviewed;       220 AA.
AC   A4AT93;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000256|SAAS:SAAS01094786};
DE            Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000256|SAAS:SAAS01094783};
GN   Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN   OrderedLocusNames=FB2170_16301 {ECO:0000313|EMBL:EAR00663.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00663.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00663.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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|HAMAP-Rule:MF_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00135, ECO:0000256|SAAS:SAAS01094789}.
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DR   EMBL; CP002157; EAR00663.1; -; Genomic_DNA.
DR   RefSeq; WP_013304466.1; NC_014472.1.
DR   STRING; 313603.FB2170_16301; -.
DR   EnsemblBacteria; EAR00663; EAR00663; FB2170_16301.
DR   KEGG; fbc:FB2170_16301; -.
DR   eggNOG; ENOG4108ZGB; Bacteria.
DR   eggNOG; COG0135; LUCA.
DR   HOGENOM; HOG000161598; -.
DR   KO; K01817; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   BioCyc; MSP313603:G1GNS-39-MONOMER; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000001602; 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; -; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001240; PRAI.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AT93.
DR   SWISS-2DPAGE; A4AT93.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00135,
KW   ECO:0000313|EMBL:EAR00663.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN       28    217       PRAI. {ECO:0000259|Pfam:PF00697}.
SQ   SEQUENCE   220 AA;  25312 MW;  259B8F71427BBABE CRC64;
     MSQYHQNIDT STRKPLKLKV CGMNLNTVEV ATLKPDYMGF IFWQPSKRCY NEESTIIPHK
     IKKVGVFVDE DIQVIIKKVK KHQLLGVQLH GKESPSFCKQ LKTELKGVEI IKVFSIKNEF
     DFSILAPFED VCDFFLFDTK GKLPGGNGYK FNWKTLNDYP STKPFFLSGG IGLDDADSIQ
     EFMQQPESQY CHAIDVNSMF EIEPGLKDIE KLKDFIKRLK
//

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