ID C0QKV6_DESAH Unreviewed; 615 AA.
AC C0QKV6;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Acd10 {ECO:0000313|EMBL:ACN16196.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:ACN16196.1};
GN Name=acd10 {ECO:0000313|EMBL:ACN16196.1};
GN OrderedLocusNames=HRM2_31130 {ECO:0000313|EMBL:ACN16196.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16196.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN16196.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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}.
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DR EMBL; CP001087; ACN16196.1; -; Genomic_DNA.
DR RefSeq; WP_015904958.1; NC_012108.1.
DR AlphaFoldDB; C0QKV6; -.
DR STRING; 177437.HRM2_31130; -.
DR KEGG; dat:HRM2_31130; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_7; -.
DR OrthoDB; 9765339at2; -.
DR Proteomes; UP000000442; Chromosome.
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:UP000000442}.
FT DOMAIN 4..30
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 37..154
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 159..266
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 466..608
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 615 AA; 67393 MW; 4905860EEB922BBB CRC64;
MAQLISDRRD IDFVLHEQLG LVDHERFAEF NKKTVDLIVS EARNLAVKEI LPTQKPGDEE
GCTFDNGRVT VPPCFKRAWE LYKEGEWLAM TDDPEVGGQG MPKLVGLAAN EYLIGANPSF
MLYSGMTHGA ATLVEAFGTD EQKRLYMKKM FSGEWGGTML LTEAEAGSDV GALSSVAKKN
ADGTYSITGT KIFISAGEHD LAKNIIHPVL ARIEGAPEGT RGISLFLVPK YRVNDDGSLG
EFNNVVCTGI EEKMGLHGNA TCTLSLGEKG ESIGTLLGAE NKGMSAMFRM MNEARAFVGL
QGFAVSTASY MYALDYARTR IQGKNILKAR QPGVKSCPII EHPDVRRQLL NMKALIEGMR
SLIYFNGKCL DIAETSEDPE QKERYGDMVE LLTPLVKGYV TDRSLEVCSH GVQVYGGYGY
IKEFPVEQLM RDSRIYMIYE GTNGIQAMDL LGRKLAMKDG KLFRDFIDEI RQVVEAAKQV
EGVKAIAARV EKAVDKLEQT AKVIGERSKS KDVMNAYSFA HPFLEVTGDV AMAWMLLWRA
MVAAPKLVKK AGSLDPEVVA AKSATNKDAA YYAGQVMTAA FFINTLLPSA LAKMDAIVEG
DSSVETMPEA AFGSR
//
