ID T0GPP7_9SPHN Unreviewed; 323 AA.
AC T0GPP7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Pyruvate dehydrogenase E1 subunit alpha {ECO:0000313|EMBL:EQB01968.1};
GN ORFNames=L485_09535 {ECO:0000313|EMBL:EQB01968.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB01968.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQB01968.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQB01968.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(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:EQB01968.1}.
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DR EMBL; ATIB01000053; EQB01968.1; -; Genomic_DNA.
DR RefSeq; WP_021244803.1; NZ_KQ130471.1.
DR AlphaFoldDB; T0GPP7; -.
DR PATRIC; fig|1114964.3.peg.1863; -.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000015524; Unassembled WGS sequence.
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; IPR029061; THDP-binding.
DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 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:EQB01968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015524}.
FT DOMAIN 14..311
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 323 AA; 34570 MW; B6E1338925B63090 CRC64;
MNGPDLQRSL QLFERMLLIR RMEERLGDLG KAGELPGNVH LYIGQEAVAT GVCAHLDDSD
WVASTHRGHG HFLAKGGDPR AMAAELMGKE TGICHGKGGS MHVADVSKGI LGANGIVGGG
VGLAVGAALG AQLDGEGRVA VVFFGDGASS QGVISEALNI AALWKLPLLL VCENNGFSQF
SPYETVNAGD IWRRAEPFGM PGALVDGNDV HAVWRVVGEA VARARSGEGA TLIEARTYRW
RTHVESEESF LAAPYRTQEE VESWKQRDPI SRLEEFLVSE DLEKDVAAIR ARVEGVTESA
ITDALNDPLP PVSRAFEDMF ANG
//
