ID A0A080MDR3_9PROT Unreviewed; 541 AA.
AC A0A080MDR3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Indole-3-pyruvate decarboxylase {ECO:0000313|EMBL:KFB78570.1};
DE EC=4.1.1.74 {ECO:0000313|EMBL:KFB78570.1};
GN Name=ipdC {ECO:0000313|EMBL:KFB78570.1};
GN ORFNames=AW06_000033 {ECO:0000313|EMBL:KFB78570.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB78570.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB78570.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000256|ARBA:ARBA00001920};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB78570.1}.
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; JDST02000002; KFB78570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080MDR3; -.
DR STRING; 1453999.AW06_000033; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR017765; IPDC.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR NCBIfam; TIGR03394; indol_phenyl_DC; 1.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KFB78570.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Pyruvate {ECO:0000313|EMBL:KFB78570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..308
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..515
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 541 AA; 58072 MW; 29BF2742FEAA70BD CRC64;
MNITESLLHA LKAHGAHEIF GIPGDFALPY FRIIEESGIL PLYTLSHEPG VGFAADASAR
YHGTLGVAAV TYGAGALNMV NAVASAFAEK SPLVILSGGP GKNDARSGLL LHHQAKTLDS
QFQIYREITC DQVRLDDAAR APADIARVLA NCRRHSRPVY IELPRDMVST PCATTPTTEP
AGPDPDALAA CVDEILGRLA AATAPVLMVG VEVRRFGLEA KAAELARRLA LPVVTSFMGR
GLLAAANAPL MGTYLGIAGA PDVTTAVESS DGLFLLGVII SDTNFGVSDK KIDLRKTIQA
LDRRVTMGYH TYDAIGLESL VDALLARTVP SDRHFDVKKQ DYPFDLPDDD APLMPLDIAT
AVNDLMRDKG RMPIASDIGD CLFTAMDMAN TELVAPGYYA TMGFGVPAGI GLQAASGERT
LILVGDGAFQ MTGWELGNCR RFGFDPIVIV FNNQSWEMLR TFQPQSGFND LDDWHFAEMA
PAMGGEGVRV STRRELKHAL AEAHATRGKF RLIEVMLPRG ALSPTLARFV TGLRRLTANP
G
//
