ID S7V9K7_DESML Unreviewed; 604 AA.
AC S7V9K7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Acetyl-CoA dehydrogenase-like C-terminal domain containing protein {ECO:0000313|EMBL:EPR41188.1};
GN ORFNames=dsmv_2196 {ECO:0000313|EMBL:EPR41188.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR41188.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR41188.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR41188.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:EPR41188.1}.
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DR EMBL; ATHJ01000077; EPR41188.1; -; Genomic_DNA.
DR RefSeq; WP_020876627.1; NZ_FUWN01000026.1.
DR AlphaFoldDB; S7V9K7; -.
DR STRING; 897.B2D07_14130; -.
DR PATRIC; fig|1121405.3.peg.1743; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9765339at2; -.
DR Proteomes; UP000014977; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000014977}.
FT DOMAIN 4..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 41..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..453
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 469..595
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 604 AA; 66451 MW; F6277EB0E61D8F60 CRC64;
MAQVIADRRD VDFVLHEQLE VGEFSKTEKF AEFTRKTVDL IINEARNLAV KEILPTQKIG
DEKGCAFDGG KVTVPEEFHR IYKLFREGEW LAMNEDPQWG GQGMPRTVAL AANDFFNGAN
YAFIMYPGLT HGAAKLVEVF GSDEQKRIFL KKMYSGEWTG TMLLTEPEAG TDVGALQTTA
VKNEDGTYAI TGNKIFISSG EHDLTENIIH PVLARIEGAP EGTRGISLFL VPKYRVNPDG
SLGEFNDVVC TGIEHKMGIH GNATCSLTLG GKGNCIGTLL GEENKGMKAM FLMMNEARAL
VGMQGFCCAS AAYLNAVNYA RERIQGKHLL QMMDANAPAV PIIQHPDIRR MLLKMKSLVE
GMRSLLYYHG YLDDLKHLSD DPEEIAKLQG MIELLTPIVK GYITDRAFEV CSEGVQVFGG
YGFISDYPQE QLLRDCRITQ IYEGTNGIQA MDLLGRKLGM NQGKPVMDLL AEMNRTIAAA
GEIPALEDFV ADFKAAVKKL GEVGMHMGMT AMSPKVLNAF AFAHPFMEVT GDVAVAWMLL
WRASIAGRKM DGAGKKDKVF YEGQIRSAEY FIKSVLPITL GKMNAILTNN GAAIEISEDA
FGGR
//
