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Database: UniProt
Entry: K9CG88_9FIRM
LinkDB: K9CG88_9FIRM
Original site: K9CG88_9FIRM 
ID   K9CG88_9FIRM            Unreviewed;       204 AA.
AC   K9CG88;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=HMPREF9161_01829 {ECO:0000313|EMBL:EKU70783.1};
OS   Selenomonas sp. F0473.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=999423 {ECO:0000313|EMBL:EKU70783.1, ECO:0000313|Proteomes:UP000009883};
RN   [1] {ECO:0000313|EMBL:EKU70783.1, ECO:0000313|Proteomes:UP000009883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0473 {ECO:0000313|EMBL:EKU70783.1,
RC   ECO:0000313|Proteomes:UP000009883};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA   Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Selenomonas sp. Oral taxon 133 strain F0473.";
RL   Submitted (SEP-2012) 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:EKU70783.1}.
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DR   EMBL; AGZT01000008; EKU70783.1; -; Genomic_DNA.
DR   RefSeq; WP_009729413.1; NZ_JH992902.1.
DR   AlphaFoldDB; K9CG88; -.
DR   STRING; 999423.HMPREF9161_01829; -.
DR   PATRIC; fig|999423.3.peg.1928; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_1_0_9; -.
DR   OrthoDB; 9786954at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000009883; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009883};
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   204 AA;  21762 MW;  F1DD49B78FBCBFAA CRC64;
     MRVKMCGMKS LAAARAAQEA GADYIGFVFA KESRRYVAPD TAREICAAIG GVEKVGVFVD
     AAPEEMNEIA AYCGLDYIQL HGHEPAEAAR RVNRPVIKAY RYGDDFDAAA ANGYPAEIIL
     IDSYVPGAAG GTGTVFRWEA AAREVARVTK PVLIAGGIVA ENVGTAMEIF HPFGVDVSGG
     LEENGEKSAE KIRMFMDAVR TAKI
//
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