ID B7GFC9_ANOFW Unreviewed; 431 AA.
AC B7GFC9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Dehydrogenase (Flavoprotein) {ECO:0000313|EMBL:ACJ33620.1};
GN OrderedLocusNames=Aflv_1250 {ECO:0000313|EMBL:ACJ33620.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ33620.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ33620.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family.
CC {ECO:0000256|ARBA:ARBA00006796}.
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DR EMBL; CP000922; ACJ33620.1; -; Genomic_DNA.
DR RefSeq; WP_012574871.1; NC_011567.1.
DR AlphaFoldDB; B7GFC9; -.
DR STRING; 491915.Aflv_1250; -.
DR GeneID; 7037504; -.
DR KEGG; afl:Aflv_1250; -.
DR PATRIC; fig|491915.6.peg.1284; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_050977_0_0_9; -.
DR Proteomes; UP000000742; Chromosome.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039651; FixC-like.
DR PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000742}.
SQ SEQUENCE 431 AA; 48544 MW; 94B94A10CEF1470C CRC64;
MSEKFDCIVV GAGPAGTACA YELAKAGVNV LLLERGEYPG AKNVMGGVLY RKMMEDIIPE
FYKEAPLERP IVEQRFMMMD KESAVTFSYK GLEWGREPYN NFTVLRAKFD QWFAEKAVEQ
GALLVCETVA VECIVENGRV VGVRTDRPDG DIYADVVVLA DGVNSLLAKQ LGFHREWRPD
EVALATMEIL KLDKNVIEDR FNLEANQGCT IEIFGDATKG IVGTGFLYTN KDTLSIGVGT
LLSGLIKHKM KPYELLEYVK NHPMIRPYIQ GSEPVEYLAH LIPEGGYHSI PKVAGNGVLV
VGDAAQLVNA IHREGSNMAM TSGRLAAETI IMAKERNDFS ESMLDQYRMK LMESFIGQDL
KKYKDATHHF ESFPQYFEQY IPMLNRAASQ MFTVDGASKW EKQKKIWHDL GSTKQKFKLA
RDMMKAWKVM K
//
