ID F3PMQ6_9BACE Unreviewed; 310 AA.
AC F3PMQ6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN ORFNames=HMPREF9445_03322 {ECO:0000313|EMBL:EGF49175.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF49175.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF49175.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF49175.1,
RC ECO:0000313|Proteomes:UP000010321};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001633};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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:EGF49175.1}.
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DR EMBL; AFBM01000034; EGF49175.1; -; Genomic_DNA.
DR RefSeq; WP_009123376.1; NZ_GL882601.1.
DR AlphaFoldDB; F3PMQ6; -.
DR STRING; 762984.SAMN05444376_0955; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_10; -.
DR OrthoDB; 9804217at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000010321; Unassembled WGS sequence.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00218; IGPS; 2.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS00614; IGPS; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 4..214
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 251..294
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT REGION 232..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 310 AA; 33929 MW; DAF894E9ECBFA9FE CRC64;
MDILSEITDH KRIEVELQKQ AVSPEQLREQ VRDLMENSPA PRRSMKRALA SSPAGIIAEF
KRRSPSKGWI YETAKADEIP AAYKAAGASA ISILTDEKFF GGSLRDIRTA RPLVDIPILR
KDFIIDEYQL LQARIAGADA VLLIAACLTQ EECADLTARA HALGLEVLLE IHSPRELAYI
SKDVDMVGVN NRNLGTFVTD VENSFRIAGQ LRQAIAGVRN ISDAQDAPDA CNISDARNVP
NAQGSSDTPR HQPLLVSESG ISHPETICRL RTAGFRGFLI GETFMKTPQP GDALKGFIQG
IEETEAQKSL
//
