ID   A0A1H3ZKA3_ALKAM        Unreviewed;       539 AA.
AC   A0A1H3ZKA3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Indolepyruvate decarboxylase {ECO:0000313|EMBL:SEA23851.1};
GN   ORFNames=SAMN04488051_102216 {ECO:0000313|EMBL:SEA23851.1};
OS   Alkalimonas amylolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX   NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA23851.1, ECO:0000313|Proteomes:UP000198773};
RN   [1] {ECO:0000313|EMBL:SEA23851.1, ECO:0000313|Proteomes:UP000198773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA23851.1,
RC   ECO:0000313|Proteomes:UP000198773};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNRM01000002; SEA23851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3ZKA3; -.
DR   STRING; 152573.SAMN04488051_102216; -.
DR   OrthoDB; 9773408at2; -.
DR   Proteomes; UP000198773; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; 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   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};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Pyruvate {ECO:0000313|EMBL:SEA23851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198773};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..111
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          389..516
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   539 AA;  59692 MW;  460F3716FD982628 CRC64;
     MNLVDALLHE LKQLQVQHIY GIPGDFVLPL FEQLQLRAQL PLVYLSHEPA AVFAADAAAR
     ISNKPAAVIL TYGAGALNAV NAVAQAYVEH VPLLVIAGYP AQAEKERQLL IHHQARRFDS
     QKKIFEEITA CQVRLDDPKT AWRQLQQACM LCQQESLPVL IEWPRNATAF DVGERPRRPK
     RLVDIEQLQA AVQAMLLRLR QARQPLLLID VDVRRFAAVQ QVEQLAKRCQ LPMLTTLLGR
     AAVDQQHANY RGIFLDQADS QSYALVEQAD LIIQLGVIPT DSNFAAHQHL FAPQKVIDIQ
     QQGCRIGEQY FVGFGIAELL DALLQQQLPH YRLPAKNTIA PVLVDKTDCT KALDPIRLMQ
     VVHQELLAQP DVLPMVADIG DCLFASLQAE PSLLLAPAFY ASMGYAIPAA LGVQLTSGLR
     PVVLVGDGAF RMTGLELGHC QRYGLNPIVI LFNNSNWEMI RAFAPKLDCA NLGCWHYAEL
     ATAMGALGLV ADDSRSLAAA IRQALQQKEQ TVLIEVRYPA GQQSKQLERF ASRFLGTAC
//