ID A0A177INB3_9CORY Unreviewed; 556 AA.
AC A0A177INB3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN ORFNames=AYJ05_09645 {ECO:0000313|EMBL:OAH29721.1};
OS Corynebacterium stationis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1705 {ECO:0000313|EMBL:OAH29721.1, ECO:0000313|Proteomes:UP000076947};
RN [1] {ECO:0000313|Proteomes:UP000076947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-15 {ECO:0000313|Proteomes:UP000076947};
RA Kaur G., Nair G.R., Mayilraj S.;
RL Submitted (FEB-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}.
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:OAH29721.1}.
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DR EMBL; LSTQ01000012; OAH29721.1; -; Genomic_DNA.
DR RefSeq; WP_066839541.1; NZ_LSTQ01000012.1.
DR AlphaFoldDB; A0A177INB3; -.
DR STRING; 1705.CA21670_12215; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000076947; 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 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:OAH29721.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076947};
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 198..313
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 556 AA; 61589 MW; 662D3B2F9CBA4759 CRC64;
MRTTVGEFII RRLKEMGIEH IIGVPGDFNL SFIEQINEAE NIEFVGACNE LNAAYAADGY
GRQSGVGALL TTYGVGELSA LNGIAGARAE HVPMVSLAGS PPLYSTEYRW NLHHSLADGD
FENMLESILP FTGAAVRITP MNVVEELDRA LHICLREKRP VHIQIPSDIT HLEIEAPDEA
LDTTLPTSDA ERLEAATARV LERIAEAKKP VFLFDQDTDR HGFTEKFRTL VDKLQIPYSQ
LTSGKGVLSE RDGLFLGSYN GKASAPGVQK IVESADLLFT TNPRFIEVNS GSFTHHLPAE
AIVNFGDQHV NVGGEFFVGI NTLELLDALI DRTKTSRKKK KEEFVYDEWE IDAEAPLTHA
RMWPRFIRFL EDDDTVIAEA GTSHIGLTPE RLPKGARYIN SPIWGAIGFT LPALLGSMLA
NRDRRHVLFI GDGSFQLTAQ ELSTILREDL KPIIVLVNNK GYTIERYILG MEEKYNDIAD
WQYAKLPQVF VPDTTMVSYQ ARTEGELEDA LSKIQTSDAG AFLEVHLDAM DAPAGLKAFG
PMTADFDFGP RGPRNP
//
