ID D3H7F3_STRM6 Unreviewed; 199 AA.
AC D3H7F3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=smi_0545 {ECO:0000313|EMBL:CBJ21795.1};
OS Streptococcus mitis (strain B6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ21795.1, ECO:0000313|Proteomes:UP000008563};
RN [1] {ECO:0000313|EMBL:CBJ21795.1, ECO:0000313|Proteomes:UP000008563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:CBJ21795.1,
RC ECO:0000313|Proteomes:UP000008563};
RX PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT "The genome of Streptococcus mitis B6--what is a commensal?";
RL PLoS ONE 5:E9426-E9426(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; FN568063; CBJ21795.1; -; Genomic_DNA.
DR RefSeq; WP_000169926.1; NC_013853.1.
DR RefSeq; YP_003445663.1; NC_013853.1.
DR AlphaFoldDB; D3H7F3; -.
DR STRING; 365659.smi_0545; -.
DR KEGG; smb:smi_0545; -.
DR PATRIC; fig|365659.3.peg.516; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_1_0_9; -.
DR OrthoDB; 9786954at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000008563; 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:CBJ21795.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 4..189
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 199 AA; 21462 MW; 72870113979324CF CRC64;
MTKVKICGLS TKEAVETAVS ARADYIGFVF APSKRQVALD QASELAKLIP AGVKKVGVFV
SPSRAELLEV IDKVGLDLVQ VHGQVADDLF ENLPCASIQA VHVDGEGHVP NSQADYLLFD
APVAGSGQTF DWAQLDTIGL TQPFFIAGGL KEDNVVKAIQ HFSPYAVDVS SGVETDGQKD
HEKIRRFIER VKNGISRTK
//
