ID Q31HH5_HYDCU Unreviewed; 212 AA.
AC Q31HH5;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=Tcr_0802 {ECO:0000313|EMBL:ABB41398.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB41398.1};
RN [1] {ECO:0000313|EMBL:ABB41398.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB41398.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA Richardson P.;
RT "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL Submitted (JUL-2006) 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}.
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DR EMBL; CP000109; ABB41398.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31HH5; -.
DR STRING; 317025.Tcr_0802; -.
DR KEGG; tcx:Tcr_0802; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_6; -.
DR OrthoDB; 9796196at2; -.
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; 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:ABB41398.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 7..207
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 212 AA; 23056 MW; 6834F7D9D7E81749 CRC64;
MQSRTRVKIC GITNTADADQ AVQAGADALG FVFYDKSPRA VTIDQAWPVF QTLPAFVTTT
ALFVNPDVAL VEKVIEDLKI DLLQFHGDES PAFCEQFSRP YIKAVRMQAE TDLEQLACQY
VSSQGLLLDT YVKGIPGGTG AAFNWDWVLP EKRQNVTLPV ILAGGLNDEN VGQAVRAVRP
WAVDVSGGVE SAPGQKSSEK IQAFIQAVNN VR
//
