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Database: UniProt
Entry: D7UYP3_LISGR
LinkDB: D7UYP3_LISGR
Original site: D7UYP3_LISGR 
ID   D7UYP3_LISGR            Unreviewed;       255 AA.
AC   D7UYP3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|ARBA:ARBA00018080, ECO:0000256|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362, ECO:0000256|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134,
GN   ECO:0000313|EMBL:EFI83460.1};
GN   ORFNames=HMPREF0556_12145 {ECO:0000313|EMBL:EFI83460.1};
OS   Listeria grayi DSM 20601.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83460.1, ECO:0000313|Proteomes:UP000010119};
RN   [1] {ECO:0000313|EMBL:EFI83460.1, ECO:0000313|Proteomes:UP000010119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83460.1,
RC   ECO:0000313|Proteomes:UP000010119};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2010) 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|ARBA:ARBA00008737,
CC       ECO:0000256|HAMAP-Rule:MF_00134}.
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:EFI83460.1}.
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DR   EMBL; ACCR02000005; EFI83460.1; -; Genomic_DNA.
DR   RefSeq; WP_003755446.1; NZ_GL538352.1.
DR   AlphaFoldDB; D7UYP3; -.
DR   STRING; 525367.HMPREF0556_12145; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_1_9; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000010119; Unassembled WGS sequence.
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_A; IGPS_A; 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; 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; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00614; IGPS; 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:UP000010119};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          4..251
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   255 AA;  28574 MW;  D932BB75FFB76249 CRC64;
     MTFLEKILTA KREEVAAMEQ ETLRPIRETY SFYDYLQAHP ERMQLIGEVK RASPSKGAIK
     LDVDPIEQAL AYERAGVAAI SVLTDPSYFK GSIEDLRQVA SRVSIPVLCK DFIIHEKQIS
     RANNAGATII LLIVAALEAK RLEELYRFAR SIGLEVLVEV HNEQELETAT KLGATIIGVN
     NRNLHSFEVD IAVSETLATK RAASGEKVCY ISESGFKTPE DVERVKQDYR AVLVGEALMR
     DDQPEKAAER LRVLR
//
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