ID Q0I8N5_SYNS3 Unreviewed; 227 AA.
AC Q0I8N5;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
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 ECO:0000313|EMBL:ABI47853.1};
GN OrderedLocusNames=sync_1984 {ECO:0000313|EMBL:ABI47853.1};
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI47853.1, ECO:0000313|Proteomes:UP000001961};
RN [1] {ECO:0000313|EMBL:ABI47853.1, ECO:0000313|Proteomes:UP000001961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311 {ECO:0000313|EMBL:ABI47853.1,
RC ECO:0000313|Proteomes:UP000001961};
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI47853.1; -; Genomic_DNA.
DR RefSeq; WP_011619899.1; NC_008319.1.
DR AlphaFoldDB; Q0I8N5; -.
DR STRING; 64471.sync_1984; -.
DR KEGG; syg:sync_1984; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_3; -.
DR OrthoDB; 9786954at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001961; Chromosome.
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:ABI47853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001961};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 9..218
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 227 AA; 25364 MW; 3C6E14EC860E1C0C CRC64;
MSDAAIALKI CGLTDHFQAC FIAAMGAQAI GVIGVDQTPR FVEEPRRRFI FMELEKLHPT
VERVWVVADP SDHAIGSALQ GEGTPTVVQL HGSETPERCI QLKQRHPKVR WWKALKLRTE
HDLSELSSFE PHTDALLLDA WSPDQLGGTG HRLNPSWFTH LHDQLKPNTV WWLAGGISAE
WVPELLSLVS PYGLDASSRL ESQPGVKDLN KVRALVQAVH DNEPLRQ
//
