DCIP_AZOBR
ID DCIP_AZOBR Reviewed; 545 AA.
AC P51852;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Indole-3-pyruvate decarboxylase;
DE Short=Indolepyruvate decarboxylase;
DE EC=4.1.1.74;
GN Name=ipdC;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sp245;
RX PubMed=8202090; DOI=10.1007/bf00280477;
RA Costacurta A., Keijers V., Vanderleyden J.;
RT "Molecular cloning and sequence analysis of an Azospirillum brasilense
RT indole-3-pyruvate decarboxylase gene.";
RL Mol. Gen. Genet. 243:463-472(1994).
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 -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; L26240; AAC36886.1; -; Unassigned_DNA.
DR PIR; S44486; S44486.
DR PDB; 2NXW; X-ray; 1.50 A; A/B=1-545.
DR PDB; 2Q5J; X-ray; 3.20 A; A/B=1-545.
DR PDB; 2Q5L; X-ray; 1.85 A; A/B=1-545.
DR PDB; 2Q5O; X-ray; 2.15 A; A/B=1-545.
DR PDB; 2Q5Q; X-ray; 1.90 A; A/B=1-545.
DR PDB; 5ABM; X-ray; 1.70 A; A/B/C/D=2-501.
DR PDBsum; 2NXW; -.
DR PDBsum; 2Q5J; -.
DR PDBsum; 2Q5L; -.
DR PDBsum; 2Q5O; -.
DR PDBsum; 2Q5Q; -.
DR PDBsum; 5ABM; -.
DR AlphaFoldDB; P51852; -.
DR SMR; P51852; -.
DR DrugBank; DB08050; 5-phenyl-2-keto-valeric acid.
DR DrugBank; DB03884; Phenylpyruvic acid.
DR BioCyc; MetaCyc:MON-20681; -.
DR BRENDA; 4.1.1.74; 611.
DR UniPathway; UPA00151; -.
DR EvolutionaryTrace; P51852; -.
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:0044281; P:small molecule metabolic process; IEA:UniProt.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR017765; IPDC.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
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; TIGR03394; indol_phenyl_DC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Thiamine pyrophosphate.
FT CHAIN 1..545
FT /note="Indole-3-pyruvate decarboxylase"
FT /id="PRO_0000090821"
FT REGION 382..460
FT /note="Thiamine pyrophosphate binding"
FT BINDING 48
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2NXW"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:2Q5Q"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2Q5J"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2NXW"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2NXW"
FT TURN 240..245
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2Q5Q"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:2Q5Q"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:2NXW"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:2NXW"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 496..508
FT /evidence="ECO:0007829|PDB:2NXW"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:2NXW"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:2NXW"
SQ SEQUENCE 545 AA; 57981 MW; C636A081729B8CD3 CRC64;
MKLAEALLRA LKDRGAQAMF GIPGDFALPF FKVAEETQIL PLHTLSHEPA VGFAADAAAR
YSSTLGVAAV TYGAGAFNMV NAVAGAYAEK SPVVVISGAP GTTEGNAGLL LHHQGRTLDT
QFQVFKEITV AQARLDDPAK APAEIARVLG AARALSRPVY LEIPRNMVNA EVEPVGDDPA
WPVDRDALAA CADEVLAAMR SATSPVLMVC VEVRRYGLEA KVAELAQRLG VPVVTTFMGR
GLLADAPTPP LGTYIGVAGD AEITRLVEES DGLFLLGAIL SDTNFAVSQR KIDLRKTIHA
FDRAVTLGYH TYADIPLAGL VDALLEGLPP SDRTTRGKEP HAYPTGLQAD GEPIAPMDIA
RAVNDRVRAG QEPLLIAADM GDCLFTAMDM IDAGLMAPGY YAGMGFGVPA GIGAQCVSGG
KRILTVVGDG AFQMTGWELG NCRRLGIDPI VILFNNASWE MLRTFQPESA FNDLDDWRFA
DMAAGMGGDG VRVRTRAELK AALDKAFATR GRFQLIEAMI PRGVLSDTLA RFVQGQKRLH
AAPRE
