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Database: UniProt
Entry: R6S7G5_9FIRM
LinkDB: R6S7G5_9FIRM
Original site: R6S7G5_9FIRM 
ID   R6S7G5_9FIRM            Unreviewed;       203 AA.
AC   R6S7G5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BN652_02544 {ECO:0000313|EMBL:CDC42602.1};
OS   Firmicutes bacterium CAG:424.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263022 {ECO:0000313|EMBL:CDC42602.1, ECO:0000313|Proteomes:UP000018167};
RN   [1] {ECO:0000313|EMBL:CDC42602.1, ECO:0000313|Proteomes:UP000018167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:424 {ECO:0000313|Proteomes:UP000018167};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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|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:CDC42602.1}.
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DR   EMBL; CBFI010000009; CDC42602.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6S7G5; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000018167; 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:CDC42602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018167};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          5..194
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
SQ   SEQUENCE   203 AA;  22460 MW;  F9B6AE9D16D09A6A CRC64;
     MTKIKLCGIS RPEDIMAVNQ WKPDYIGFVF YKKSVRCVSP ENARRLKEQL LPGILSVGVF
     VNEAPEVIAE LLEEGVIDAA QLHGQESSQY LHTLRGLTSK PLIQAIQIRS EKDLYKTAYS
     TADFLLLDSG AGTGQTFDWN LLKNIRQDFF LAGGLDAQNV ADAICQVHPY GVDVSSGIET
     NGKKDKEKIA AFMAAVRKRG EKL
//
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