ID I2AAY2_9MYCO Unreviewed; 360 AA.
AC I2AAY2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=PdhA {ECO:0000313|EMBL:AFJ34456.1};
GN ORFNames=W7S_07385 {ECO:0000313|EMBL:AFJ34456.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ34456.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ34456.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ34456.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP003491; AFJ34456.1; -; Genomic_DNA.
DR AlphaFoldDB; I2AAY2; -.
DR KEGG; mmm:W7S_07385; -.
DR PATRIC; fig|1168287.3.peg.1508; -.
DR HOGENOM; CLU_029393_1_0_11; -.
DR Proteomes; UP000002868; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 42..312
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 360 AA; 39338 MW; 03868FB3F9B688E6 CRC64;
MSSMAMAVDL EPVQLVAADG SPTSERRYGR DLPAETLSWL YELMVITREL DAEFVNLKRQ
GELALFASCR GQEAAQIGAA ACLRKTDWLF PQYRELGAFL VRGIPPGHVG AVWRGTWHGG
LEFTKKCCAP LSIPIGTQTL HAVGAAMAAQ RLGEDSVTLA FLGDGATSTG DVHEALNFAA
VFTTPCVFFV QNNQWAISTP IHKQTAAPSL AHKAIGYGMP GVRVDGNDVL ACYAVTAEAA
ARARAGGGPT LIEAITYRMG PHTTSDDPSR YRTQDEVDHW AALDPIARYR SYLRAQGLWS
ERLEERVIGR AQRMRTELRD GVVDAPDFDI DEVFTSVYAE ITPGLQAQRQ QLRAELDRSD
//
