TRPC_THEMA
ID TRPC_THEMA Reviewed; 252 AA.
AC Q56319;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE Short=IGPS;
DE EC=4.1.1.48;
GN Name=trpC; OrderedLocusNames=TM_0140;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x;
RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.;
RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the
RT hyperthermophile Thermotoga maritima.";
RL EMBO J. 14:4395-4402(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35233.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92729; CAA63389.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35233.1; ALT_INIT; Genomic_DNA.
DR PIR; S59047; S59047.
DR RefSeq; NP_227955.1; NC_000853.1.
DR PDB; 1I4N; X-ray; 2.50 A; A/B=2-252.
DR PDB; 1J5T; X-ray; 3.00 A; A=24-252.
DR PDBsum; 1I4N; -.
DR PDBsum; 1J5T; -.
DR AlphaFoldDB; Q56319; -.
DR SMR; Q56319; -.
DR STRING; 243274.THEMA_04105; -.
DR EnsemblBacteria; AAD35233; AAD35233; TM_0140.
DR KEGG; tma:TM0140; -.
DR PATRIC; fig|243274.5.peg.139; -.
DR eggNOG; COG0134; Bacteria.
DR InParanoid; Q56319; -.
DR OMA; RGPHDLI; -.
DR BioCyc; MetaCyc:MON-343; -.
DR BRENDA; 4.1.1.48; 6331.
DR SABIO-RK; Q56319; -.
DR UniPathway; UPA00035; UER00043.
DR EvolutionaryTrace; Q56319; -.
DR Proteomes; UP000008183; 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_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; 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; Direct protein sequencing; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..252
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154266"
FT CONFLICT 226
FT /note="N -> K (in Ref. 1; CAA63389)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:1I4N"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1I4N"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1I4N"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1I4N"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1I4N"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1J5T"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:1I4N"
SQ SEQUENCE 252 AA; 28660 MW; AA60B8E28BC043DF CRC64;
MRRLWEIVEA KKKDILEIDG ENLIVQRRNH RFLEVLSGKE RVKIIAEFKK ASPSAGDINA
DASLEDFIRM YDELADAISI LTEKHYFKGD PAFVRAARNL TCRPILAKDF YIDTVQVKLA
SSVGADAILI IARILTAEQI KEIYEAAEEL GMDSLVEVHS REDLEKVFSV IRPKIIGINT
RDLDTFEIKK NVLWELLPLV PDDTVVVAES GIKDPRELKD LRGKVNAVLV GTSIMKAENP
RRFLEEMRAW SE
