ID Q0RYG9_RHOJR Unreviewed; 317 AA.
AC Q0RYG9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Probable acetoin dehydrogenase alpha subunit {ECO:0000313|EMBL:ABG99667.1};
DE EC=1.1.1.303 {ECO:0000313|EMBL:ABG99667.1};
GN OrderedLocusNames=RHA1_ro08623 {ECO:0000313|EMBL:ABG99667.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000313|EMBL:ABG99667.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG99667.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000432; ABG99667.1; -; Genomic_DNA.
DR RefSeq; WP_007299722.1; NC_008269.1.
DR AlphaFoldDB; Q0RYG9; -.
DR KEGG; rha:RHA1_ro08623; -.
DR PATRIC; fig|101510.16.peg.7968; -.
DR HOGENOM; CLU_029393_5_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
DR GO; GO:0052587; F:diacetyl reductase ((R)-acetoin forming) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABG99667.1}; Plasmid {ECO:0000313|EMBL:ABG99667.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 11..307
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 317 AA; 33494 MW; 7198FCD0F1EBEB13 CRC64;
MTEPLLAHYR QMYRIRVLEN EILRLRKIEE VVGSVHLCNG QEAIYVGAAA GLDLSRDAVF
PTYRGHGWAL ALGATMHSIL AELLGRSTGT NGGRGGSAYF STPDTAMYGE NSIVGAGAPI
AAGAALAATF DGSGRVAVAA FGDGALNQGA VHEAMNFAAV QQLPIIFLVE NNHYSEMTPI
VDMVKNPVLF KRAAAYGITG ARIDGNDPIA VRDAVSKAAQ HARAGKGPVL LEAMTHRIVG
HYIGDAQQYR PAGEIDDIEA DEPLVRAARN LLQESGVTQT ELDALIADVN DEVRAASLAA
LADPVADPTT VLEHLYA
//
