ID K9QK03_9NOSO Unreviewed; 285 AA.
AC K9QK03;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
GN Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN ORFNames=Nos7107_4623 {ECO:0000313|EMBL:AFY45152.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY45152.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY45152.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY45152.1,
RC ECO:0000313|Proteomes:UP000010381};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-2012) 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, ECO:0000256|HAMAP-
CC Rule:MF_00134};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|HAMAP-Rule:MF_00134}.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC Rule:MF_00134}.
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DR EMBL; CP003548; AFY45152.1; -; Genomic_DNA.
DR RefSeq; WP_015115345.1; NC_019676.1.
DR AlphaFoldDB; K9QK03; -.
DR STRING; 317936.Nos7107_4623; -.
DR KEGG; nos:Nos7107_4623; -.
DR PATRIC; fig|317936.3.peg.5016; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_3; -.
DR InParanoid; K9QK03; -.
DR OrthoDB; 9804217at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000010381; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00134_B; IGPS_B; 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; 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; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00134};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00134};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00134};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00134}.
FT DOMAIN 16..275
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
SQ SEQUENCE 285 AA; 31712 MW; 676F507BD1DCBE46 CRC64;
MIYPMTTVNS HLQPMLREIV WQKKQEVAQI QQHMSLASLQ RQLTAAPTVR DFLTALQQSP
HNPSLIAEIQ KASPGYGMIR ADFDAIAIAK AYQRAGAACI SVFTERTFFQ GSFESLRIIR
HKVSVPLLCK EFIIDPCQIY LARAAGADAV LLIAAILTDR QLQDFQRIIH YLGMNALIEV
HTLAELDRVL QLDDVRLIGI NNQSLVDFTV DIGTTQRLLA ARRSQIQNLG AIVVSESGLY
THTDLSLMAE AGTNAVLIGE SLIKETDIEQ AVRRLLNIDS STFKD
//
