TRPF_MARMS
ID TRPF_MARMS Reviewed; 205 AA.
AC A6VWY4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; OrderedLocusNames=Mmwyl1_2041;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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:0000255|HAMAP-Rule:MF_00135};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
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DR EMBL; CP000749; ABR70963.1; -; Genomic_DNA.
DR RefSeq; WP_012069742.1; NC_009654.1.
DR AlphaFoldDB; A6VWY4; -.
DR SMR; A6VWY4; -.
DR STRING; 400668.Mmwyl1_2041; -.
DR EnsemblBacteria; ABR70963; ABR70963; Mmwyl1_2041.
DR KEGG; mmw:Mmwyl1_2041; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_6; -.
DR OMA; CEIMEIC; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
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_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW Tryptophan biosynthesis.
FT CHAIN 1..205
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000197110"
SQ SEQUENCE 205 AA; 21849 MW; 699E2FF2A24D15D4 CRC64;
MNCRVKICGI TNLDDAMVAC RYGADALGFV FYEKSPRYVA PDMANAIVAQ LPPFIIPVAL
FVDADTSLVN SVISGSSRWT IQFHGSESES ECISYQRPYI KALRIQRGDD VAALVDQYPS
ASAMLLDAYK AGVPGGTGEV FDWSLIPIGL SKPIVLAGGL TPSNVKQAIK QVKPYAVDVS
GGVELSKGIK SEPLVQEFIS GAKCG