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Database: UniProt
Entry: A6UGP7_SINMW
LinkDB: A6UGP7_SINMW
Original site: A6UGP7_SINMW 
ID   A6UGP7_SINMW            Unreviewed;       231 AA.
AC   A6UGP7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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   OrderedLocusNames=Smed_4019 {ECO:0000313|EMBL:ABR62827.1};
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG   Plasmid pSMED01 {ECO:0000313|EMBL:ABR62827.1,
OG   ECO:0000313|Proteomes:UP000001108}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR62827.1, ECO:0000313|Proteomes:UP000001108};
RN   [1] {ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR62827.1, ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|EMBL:ABR62827.1,
RC   ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
RX   PubMed=21304680; DOI=10.4056/sigs.43526;
RA   Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA   Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT   "Complete genome sequence of the Medicago microsymbiont Ensifer
RT   (Sinorhizobium) medicae strain WSM419.";
RL   Stand. Genomic Sci. 2:77-86(2010).
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}.
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DR   EMBL; CP000739; ABR62827.1; -; Genomic_DNA.
DR   RefSeq; YP_001312760.1; NC_009620.1.
DR   AlphaFoldDB; A6UGP7; -.
DR   KEGG; smd:Smed_4019; -.
DR   PATRIC; fig|366394.8.peg.466; -.
DR   HOGENOM; CLU_076364_2_1_5; -.
DR   OrthoDB; 9796196at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000001108; Plasmid pSMED01.
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:ABR62827.1};
KW   Plasmid {ECO:0000313|EMBL:ABR62827.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          11..226
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
SQ   SEQUENCE   231 AA;  24540 MW;  B7092D717C26B1DE CRC64;
     MQTETALKIQ IYTMQTAAEA VAAAAAGVDY LGVTPSNRGL PGEITFAKAR EIVDALEGKA
     QRVALSVESN LDDIAAMVEA VRPDVLHLCG DIALVTPEQV KVLRSRLSAE HPALRILQAI
     PMTGPEALDQ AAAFEPFVDM FILDSVAPHI GGIGAAGVTH DWSLSREIVA RSRLPVILAG
     GLRPDNVRAA IEAVRPWGVD SLTHTNRPLP EGGFRKDLDK IAAFVEAARA T
//
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