TRPC_SACS2
ID TRPC_SACS2 Reviewed; 248 AA.
AC Q06121; P50385;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE Short=IGPS;
DE EC=4.1.1.48;
GN Name=trpC; OrderedLocusNames=SSO0895;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8416906; DOI=10.1128/jb.175.1.299-302.1993;
RA Tutino M.L., Scarano G., Marino G., Sannia G., Cubellis M.V.;
RT "Tryptophan biosynthesis genes trpEGC in the thermoacidophilic
RT archaebacterium Sulfolobus solfataricus.";
RL J. Bacteriol. 175:299-302(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RA Tutino M.L., Cubellis M., Sannia G., Marino G.;
RT "The tryptophan operon in Sulfolobus solfataricus.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8747456; DOI=10.1016/s0969-2126(01)00267-2;
RA Hennig M., Darimont B., Kirschner K., Jansonius J.N.;
RT "2.0-A structure of indole-3-glycerol phosphate synthase from the
RT hyperthermophile Sulfolobus solfataricus: possible determinants of protein
RT stability.";
RL Structure 3:1295-1306(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8893859; DOI=10.1006/jmbi.1996.0531;
RA Knoechel T.R., Hennig M., Merz A., Darimont B., Kirschner K.,
RA Jansonius J.N.;
RT "The crystal structure of indole-3-glycerol phosphate synthase from the
RT hyperthermophilic archaeon Sulfolobus solfataricus in three different
RT crystal forms: effects of ionic strength.";
RL J. Mol. Biol. 262:502-515(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RA Hennig M., Darimont B., Kirschner K., Jansonius J.N.;
RT "The catalytic mechanism of indole-3-glycerolphosphate synthase: crystal
RT structure of substrate, product and substrate analogue bound to the enzyme
RT from Sulfolobus solfataricus.";
RL Submitted (FEB-1998) to the PDB data bank.
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
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DR EMBL; M98048; AAA73381.1; -; Genomic_DNA.
DR EMBL; Z50014; CAA90313.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41177.1; -; Genomic_DNA.
DR PIR; C40635; C40635.
DR PIR; S50179; S50179.
DR RefSeq; WP_009992313.1; NC_002754.1.
DR PDB; 1A53; X-ray; 2.00 A; A=2-248.
DR PDB; 1IGS; X-ray; 2.00 A; A=1-248.
DR PDB; 1JUK; X-ray; 2.50 A; A=1-248.
DR PDB; 1JUL; X-ray; 2.00 A; A=1-248.
DR PDB; 1LBF; X-ray; 2.05 A; A=2-248.
DR PDB; 1LBL; X-ray; 2.40 A; A=2-248.
DR PDB; 2C3Z; X-ray; 2.80 A; A=27-248.
DR PDB; 3NYZ; X-ray; 1.51 A; A/B=1-248.
DR PDB; 3NZ1; X-ray; 1.56 A; A=1-248.
DR PDB; 3TC6; X-ray; 1.60 A; A=1-245.
DR PDB; 3TC7; X-ray; 1.50 A; A=1-245.
DR PDB; 4A29; X-ray; 1.10 A; A=1-247.
DR PDB; 4A2R; X-ray; 1.30 A; A=1-245.
DR PDB; 4A2S; X-ray; 1.40 A; A=1-245.
DR PDB; 4IWW; X-ray; 2.30 A; A/B=2-248.
DR PDB; 4IX0; X-ray; 2.50 A; A=2-248.
DR PDB; 4LNY; X-ray; 1.93 A; A=1-247.
DR PDB; 4OU1; X-ray; 1.25 A; A=1-247.
DR PDB; 5AN7; X-ray; 1.10 A; A=1-247.
DR PDB; 5AOU; X-ray; 1.10 A; A=1-245.
DR PDB; 5K7J; X-ray; 1.39 A; A/B=2-248.
DR PDB; 6NW4; X-ray; 3.00 A; A=2-248.
DR PDBsum; 1A53; -.
DR PDBsum; 1IGS; -.
DR PDBsum; 1JUK; -.
DR PDBsum; 1JUL; -.
DR PDBsum; 1LBF; -.
DR PDBsum; 1LBL; -.
DR PDBsum; 2C3Z; -.
DR PDBsum; 3NYZ; -.
DR PDBsum; 3NZ1; -.
DR PDBsum; 3TC6; -.
DR PDBsum; 3TC7; -.
DR PDBsum; 4A29; -.
DR PDBsum; 4A2R; -.
DR PDBsum; 4A2S; -.
DR PDBsum; 4IWW; -.
DR PDBsum; 4IX0; -.
DR PDBsum; 4LNY; -.
DR PDBsum; 4OU1; -.
DR PDBsum; 5AN7; -.
DR PDBsum; 5AOU; -.
DR PDBsum; 5K7J; -.
DR PDBsum; 6NW4; -.
DR AlphaFoldDB; Q06121; -.
DR SMR; Q06121; -.
DR STRING; 273057.SSO0895; -.
DR EnsemblBacteria; AAK41177; AAK41177; SSO0895.
DR GeneID; 44129825; -.
DR KEGG; sso:SSO0895; -.
DR PATRIC; fig|273057.12.peg.898; -.
DR eggNOG; arCOG01088; Archaea.
DR HOGENOM; CLU_034247_0_1_2; -.
DR InParanoid; Q06121; -.
DR OMA; RGPHDLI; -.
DR PhylomeDB; Q06121; -.
DR BioCyc; MetaCyc:MON-3602; -.
DR BRENDA; 4.1.1.48; 6163.
DR SABIO-RK; Q06121; -.
DR UniPathway; UPA00035; UER00043.
DR EvolutionaryTrace; Q06121; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00134_A; IGPS_A; 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; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Decarboxylase; Lyase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..248
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154302"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3NYZ"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2C3Z"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:4A29"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4A29"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4A29"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4A29"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4A29"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:4A29"
SQ SEQUENCE 248 AA; 28588 MW; 919E2AEEE68DDF65 CRC64;
MPRYLKGWLK DVVQLSLRRP SFRASRQRPI ISLNERILEF NKRNITAIIA EYKRKSPSGL
DVERDPIEYS KFMERYAVGL SILTEEKYFN GSYETLRKIA SSVSIPILMK DFIVKESQID
DAYNLGADTV LLIVKILTER ELESLLEYAR SYGMEPLIEI NDENDLDIAL RIGARFIGIN
SRDLETLEIN KENQRKLISM IPSNVVKVAE SGISERNEIE ELRKLGVNAF LIGSSLMRNP
EKIKEFIL
