ID A4AFX0_9ACTN Unreviewed; 327 AA.
AC A4AFX0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Acetoin dehydrogenase (TPP-dependent) alpha chain {ECO:0000313|EMBL:EAR25876.1};
GN ORFNames=A20C1_08348 {ECO:0000313|EMBL:EAR25876.1};
OS marine actinobacterium PHSC20C1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25876.1, ECO:0000313|Proteomes:UP000003868};
RN [1] {ECO:0000313|EMBL:EAR25876.1, ECO:0000313|Proteomes:UP000003868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25876.1,
RC ECO:0000313|Proteomes:UP000003868};
RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR25876.1}.
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DR EMBL; AAOB01000002; EAR25876.1; -; Genomic_DNA.
DR AlphaFoldDB; A4AFX0; -.
DR STRING; 312284.A20C1_08348; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000003868; 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; 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:UP000003868}.
FT DOMAIN 25..313
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 327 AA; 34563 MW; FDD5E109ADDE9916 CRC64;
MTYHPVNPTL ADPLPADALE LLRSMYEIRF FEDEIMGLFS QNLVRGSTHL CQGQEAVTVG
VCSALSPGDT MTCTYRGHGA VLAMGAPLDR AFGEILGRAG GLCGGKGGSM HLADVSVGAL
GSNAIVGGHL PTTVGAALAA SYRGTSEVSV AFFGDGSTNI GAFHESLNLA SIWKLPAIFV
IENNQYGEYS TLASTTPIER LSDRAASYGM PGVFVDGNDV IAMRSATKTA VERARAGEGP
TLIEADTYRH SGHSRSDPAK YRPEEEVKSW FARDPIVQLR NAIEASGGAD AAAEVERTAH
TDVDAARDLA LTWPEPELSA GMEHIYS
//