ID N1UY99_9MICC Unreviewed; 371 AA.
AC N1UY99;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000313|EMBL:EMY32754.1};
GN ORFNames=D477_018456 {ECO:0000313|EMBL:EMY32754.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY32754.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY32754.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY32754.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EMY32754.1}.
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DR EMBL; ANPE02000234; EMY32754.1; -; Genomic_DNA.
DR RefSeq; WP_005272924.1; NZ_ANPE02000234.1.
DR AlphaFoldDB; N1UY99; -.
DR Proteomes; UP000010729; Unassembled WGS sequence.
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};
KW Pyruvate {ECO:0000313|EMBL:EMY32754.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010729}.
FT DOMAIN 48..317
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 371 AA; 40215 MW; 523EA2C049C6D025 CRC64;
MSLHGRGPVP DENLVQLLRP DGTRTDGSGY TEWLGDIDGA ALRGLYEDMV VVRRIDQEAT
ALQRQGELAL WPPLLGQEAA QIGSGRALRQ DDFVFSSYRE NGVAYCRGVG YADLLRVWRG
NAPSGWDPYA VNMATPQVII GAQTLHATGY AMATKFDGAD AVAVAYFGDG ATSQGDANEA
MVFAASFQAP VVFFCQNNQW AISEPVRLQA QRDIADRAPG FGIPSVRVDG NDVLASLAVT
RQALDRARGG GGPSFIEAVT YRMGPHTTAD DPSRYRDPNE LEDWKSRDPI DRLARLLKAE
GLLDEEFASQ AKDTADRAAA ELREACVTMP EPGELDVFDN VYATPHTVLA EQKEEYRRYL
ASLAAAPGGT A
//
