ID A0A2Z5QXB2_9MICC Unreviewed; 565 AA.
AC A0A2Z5QXB2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN ORFNames=RA11412_0565 {ECO:0000313|EMBL:BAV86864.1};
OS Rothia aeria.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=172042 {ECO:0000313|EMBL:BAV86864.1, ECO:0000313|Proteomes:UP000250241};
RN [1] {ECO:0000313|EMBL:BAV86864.1, ECO:0000313|Proteomes:UP000250241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11412 {ECO:0000313|EMBL:BAV86864.1,
RC ECO:0000313|Proteomes:UP000250241};
RA Nambu T.;
RT "Genome sequence of Rothia aeria strain JCM11412.";
RL Submitted (OCT-2016) 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; AP017895; BAV86864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5QXB2; -.
DR KEGG; raj:RA11412_0565; -.
DR Proteomes; UP000250241; 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; 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.
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:BAV86864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250241};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 565 AA; 60477 MW; C8B80A3917D0C0C2 CRC64;
MTYNVGNYLL DRLAELGVNH LFGVPGDFNL QFLDDVLAHP DISWVGNANE LNAGYAADGY
ARIRGVGALL TTYGVGELSA INATAGSYAE NVPVIHIVGA PSLAAQNAHL RMHHTLGDGD
FQHFVRMAAE VSAATAVLQP ATAASDIDRV LRDAVLHHKP GYIMLPVDVA VAAAAKPAAP
LNVNLRVSSP SVEHEFRVAA TEFLRDKKAA VLADIMTERL GATENLRDLV ESTGLPFATM
IWGKSILDET SPQFAGVYIG GLSASTTRAT VEEAQALILA GVQFTDTTSG LYTHQIDAAR
TITVDAEQTQ IGRKIFAPLA FTDALRILKE AALDAGVRPA EHTVPAHGTT LPDYGEPEPT
GVPACGDRPL TQQALWSIIP SHLDSRNNVV VEMGTSFFGM AQQSFPAQTR FIGMPLWGSI
GYSLPALLGT ALADEQARGV LFIGDGSAQL TVQELGSIFR HRLTPVIFLI NNDGYTIERS
IHGPNATYND IATYDWQKIP AAFGGTDQTV LVLRAATVDE LATACATARE TRDKAVFIEV
VTDRDDMPQL LRDFGAMAAA INRKE
//
