ID R5AF12_9FIRM Unreviewed; 333 AA.
AC R5AF12;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acetoin dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:CCX40454.1};
GN ORFNames=BN453_01390 {ECO:0000313|EMBL:CCX40454.1};
OS Firmicutes bacterium CAG:102.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX40454.1, ECO:0000313|Proteomes:UP000018112};
RN [1] {ECO:0000313|EMBL:CCX40454.1, ECO:0000313|Proteomes:UP000018112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:102 {ECO:0000313|EMBL:CCX40454.1,
RC ECO:0000313|Proteomes:UP000018112};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX40454.1}.
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DR EMBL; CAWG010000073; CCX40454.1; -; Genomic_DNA.
DR AlphaFoldDB; R5AF12; -.
DR STRING; 1262998.BN453_01390; -.
DR Proteomes; UP000018112; 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 Reference proteome {ECO:0000313|Proteomes:UP000018112}.
FT DOMAIN 19..315
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 35926 MW; E7D6D7B2B4AEE19E CRC64;
MASKGKKYPK EMLLDMYKTM LSIRAFETKA AECFTKGMLA GNIHLCIGQE AVPTGACYAL
EPEDYMTSTH RGHGHCIAKG ASLDKMLAEL FGKKTGYCQG KGGSMHIADV AGLHSLGANG
IVGAGIPIAA GSALVSKIKG DKHVTLCFFG DSASNQGTFH EAVNMAAAWK LPVVFLCENN
SYGVSVNIHS VTNTDTIAVR AQAYNIPGKT VDGNDPVTVY EAVKEAVDYA REGNGPSIVE
CMTFRHQGHY CGDPANYRPA SYMEEAHKKD AIPNMRKRLL DGVATEEEIL AVEKAVEDEM
EAAYQFANES AYPDPSEATT DVYFSDNERS VVR
//