DCIP_ENTCL
ID DCIP_ENTCL Reviewed; 552 AA.
AC P23234;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Indole-3-pyruvate decarboxylase;
DE Short=Indolepyruvate decarboxylase;
DE EC=4.1.1.74;
GN Name=ipdC;
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FERM BP-1529;
RX PubMed=2034209; DOI=10.1007/bf00273581;
RA Koga J., Adachi T., Hidaka H.;
RT "Molecular cloning of the gene for indolepyruvate decarboxylase from
RT Enterobacter cloacae.";
RL Mol. Gen. Genet. 226:10-16(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH THIAMINE
RP PYROPHOSPHATE AND MAGNESIUM, AND HOMOTETRAMERIZATION.
RX PubMed=12752451; DOI=10.1046/j.1432-1033.2003.03601.x;
RA Schuetz A., Sandalova T., Ricagno S., Huebner G., Koenig S., Schneider G.;
RT "Crystal structure of thiamindiphosphate-dependent indolepyruvate
RT decarboxylase from Enterobacter cloacae, an enzyme involved in the
RT biosynthesis of the plant hormone indole-3-acetic acid.";
RL Eur. J. Biochem. 270:2312-2321(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde;
CC Xref=Rhea:RHEA:18017, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:18086; EC=4.1.1.74;
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Note=Binds 1 metal ion per subunit.;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Note=Binds 1 thiamine pyrophosphate per subunit.;
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12752451}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; D90214; BAA14242.1; -; Genomic_DNA.
DR PIR; S16013; S16013.
DR PDB; 1OVM; X-ray; 2.65 A; A/B/C/D=1-552.
DR PDBsum; 1OVM; -.
DR AlphaFoldDB; P23234; -.
DR SMR; P23234; -.
DR STRING; 1399774.JDWH01000004_gene3808; -.
DR DrugBank; DB01987; Cocarboxylase.
DR eggNOG; COG3961; Bacteria.
DR BioCyc; MetaCyc:MON-7781; -.
DR BRENDA; 4.1.1.74; 155.
DR SABIO-RK; P23234; -.
DR UniPathway; UPA00151; -.
DR EvolutionaryTrace; P23234; -.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR017764; IPDC_Enterobacteriaceae.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR012110; TPP_enzyme.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43452; PTHR43452; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR03393; indolpyr_decarb; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Thiamine pyrophosphate.
FT CHAIN 1..552
FT /note="Indole-3-pyruvate decarboxylase"
FT /id="PRO_0000090822"
FT REGION 385..466
FT /note="Thiamine pyrophosphate binding"
FT BINDING 52
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:12752451"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12752451"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12752451"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1OVM"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1OVM"
FT TURN 289..295
FT /evidence="ECO:0007829|PDB:1OVM"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1OVM"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 412..423
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 435..441
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 444..450
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 456..464
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 466..471
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1OVM"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 507..517
FT /evidence="ECO:0007829|PDB:1OVM"
FT STRAND 521..529
FT /evidence="ECO:0007829|PDB:1OVM"
FT HELIX 537..550
FT /evidence="ECO:0007829|PDB:1OVM"
SQ SEQUENCE 552 AA; 60024 MW; DAC80952738D3729 CRC64;
MRTPYCVADY LLDRLTDCGA DHLFGVPGDY NLQFLDHVID SPDICWVGCA NELNASYAAD
GYARCKGFAA LLTTFGVGEL SAMNGIAGSY AEHVPVLHIV GAPGTAAQQR GELLHHTLGD
GEFRHFYHMS EPITVAQAVL TEQNACYEID RVLTTMLRER RPGYLMLPAD VAKKAATPPV
NALTHKQAHA DSACLKAFRD AAENKLAMSK RTALLADFLV LRHGLKHALQ KWVKEVPMAH
ATMLMGKGIF DERQAGFYGT YSGSASTGAV KEAIEGADTV LCVGTRFTDT LTAGFTHQLT
PAQTIEVQPH AARVGDVWFT GIPMNQAIET LVELCKQHVH AGLMSSSSGA IPFPQPDGSL
TQENFWRTLQ TFIRPGDIIL ADQGTSAFGA IDLRLPADVN FIVQPLWGSI GYTLAAAFGA
QTACPNRRVI VLTGDGAAQL TIQELGSMLR DKQHPIILVL NNEGYTVERA IHGAEQRYND
IALWNWTHIP QALSLDPQSE CWRVSEAEQL ADVLEKVAHH ERLSLIEVML PKADIPPLLG
ALTKALEACN NA
