TRPC_ZYMMT
ID TRPC_ZYMMT Reviewed; 264 AA.
AC Q9XBM3; F8ERZ8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE Short=IGPS;
DE EC=4.1.1.48;
GN Name=trpC; OrderedLocusNames=Zymop_0671;
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 / NCIMB
RC 11200 / NRRL B-4491 / Barker I;
RA Eddy C.K., Johnson G.;
RT "The trpC gene from Zymomonas mobilis encoding indole-3-glycerol phosphate
RT synthase.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 / NCIMB
RC 11200 / NRRL B-4491 / Barker I;
RX PubMed=21742897; DOI=10.1128/jb.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF167440; AAD45395.1; -; Genomic_DNA.
DR EMBL; CP002865; AEI37573.1; -; Genomic_DNA.
DR RefSeq; WP_013933972.1; NC_015709.1.
DR AlphaFoldDB; Q9XBM3; -.
DR SMR; Q9XBM3; -.
DR STRING; 579138.Zymop_0671; -.
DR EnsemblBacteria; AEI37573; AEI37573; Zymop_0671.
DR KEGG; zmp:Zymop_0671; -.
DR PATRIC; fig|579138.3.peg.706; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_5; -.
DR OMA; RGPHDLI; -.
DR OrthoDB; 1789381at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000491; 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; -; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW Lyase; Tryptophan biosynthesis.
FT CHAIN 1..264
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154288"
FT CONFLICT 14..15
FT /note="RH -> EF (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..19
FT /note="DK -> ER (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 22..37
FT /note="HISETDLYNLTKNQTA -> QIGNNALLDLIKAQTQ (in Ref. 1;
FT AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="D -> E (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..55
FT /note="EGKFS -> RGQFG (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="P -> S (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..84
FT /note="EPILHARSYQ -> TPAAHAHDYE (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="Q -> R (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..117
FT /note="NEVTLP -> KAVKLPV (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..151
FT /note="EDN -> DDQ (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> D (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="I -> V (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="TQ -> HD (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="R -> K (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..211
FT /note="IKQ -> VGS (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="E -> D (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..226
FT /note="QT -> PN (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..237
FT /note="NQHN -> QRHD (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..258
FT /note="KDVKQATR -> DDLRKATK (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> S (in Ref. 1; AAD45395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29628 MW; F855566E2E6223C8 CRC64;
MSNILTEICA TKARHVADKK KHISETDLYN LTKNQTAPRG FRAALDKKRA EGKFSLIAEI
KKASPSKGLI RPDFEPILHA RSYQEGGAAC LSVLTDQPYF QGHEDYLIAA RNEVTLPVLR
KDFMIDPWQV TEARAIGADA ILIIVAALED NQMQEIEAAA LEYGMDALIE VHSTQEMERA
LRLKSRLIGV NNRDLRDFSV SFDRTYELIK QAPKECTFVA ESGIQTHDDL VAMNQHNIGC
FLVGETLMRQ KDVKQATRDL LGLN
