ID A0A223S538_9ACTN Unreviewed; 567 AA.
AC A0A223S538;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN ORFNames=CDO52_11105 {ECO:0000313|EMBL:ASU83252.1};
OS Nocardiopsis gilva YIM 90087.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1235441 {ECO:0000313|EMBL:ASU83252.1, ECO:0000313|Proteomes:UP000215005};
RN [1] {ECO:0000313|EMBL:ASU83252.1, ECO:0000313|Proteomes:UP000215005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90087 {ECO:0000313|EMBL:ASU83252.1,
RC ECO:0000313|Proteomes:UP000215005};
RA Yin M., Tang S.;
RT "The complete genome sequence of Nocardiopsis gilva YIM 90087.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decarboxylates branched-chain and aromatic alpha-keto acids
CC to aldehydes. {ECO:0000256|ARBA:ARBA00002938}.
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; CP022753; ASU83252.1; -; Genomic_DNA.
DR RefSeq; WP_017617178.1; NZ_CP022753.1.
DR AlphaFoldDB; A0A223S538; -.
DR KEGG; ngv:CDO52_11105; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000215005; Chromosome.
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 CDD; cd02005; TPP_PDC_IPDC; 1.
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; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:ASU83252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215005};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 567 AA; 58988 MW; D32BC65E372B55EB CRC64;
MSENLEANMA AEMTVGDYLL HRLAEAGVST LFGVPGDYNL AFLDHVIADE RITWTGSANE
LNAAYAADGY ARVNGVGALL TTYGVGELSA INGIAGSYAE YLPVLHIVGA PSTSAQAAGA
LNHHTLGDGD YGHFARAQAE VTVAQAYLTR GNAAAEIDRV IATSLRERRP GYIAIPTDVA
AAPIDPPAAP LVVPAADTSA RVLRDFLADA RRLLEGADSA TVLADFLADR FDARGELRAL
CDAGNFPQAT LSLGKGVLDE SDPRFVGVYT GGVGDARVRA AVEQADVLIA AGVRFTDTIT
AGFSHDIDPA RMIDLQPFSA SIGERRYAPL PLGAALEGLA DLAASLGRDW SRSPAPAPET
VSDAAADTAA LDGELGQADL WRAVRGFLRP GDIVVAEQGT AFFGACTVPL PSGATFIGQP
LWGSIGFTLP AAFGAQHAAP DRRVVLLIGD GSALLTAQEI GSMVRDGQQP VIVVINNDGY
TVERAIHGPH ERYNDIPKWD WTLVPRAMGA GTDALTLRAT TPGEFAEALA AADSADRLAL
VEAVLPKLGL PDLLNGVSAA IAEANAE
//
