ID A0A495A872_9BACI Unreviewed; 390 AA.
AC A0A495A872;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RKQ35804.1};
GN ORFNames=D8M06_05990 {ECO:0000313|EMBL:RKQ35804.1};
OS Oceanobacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ35804.1, ECO:0000313|Proteomes:UP000269301};
RN [1] {ECO:0000313|EMBL:RKQ35804.1, ECO:0000313|Proteomes:UP000269301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ35804.1,
RC ECO:0000313|Proteomes:UP000269301};
RX PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT bacterium from a hypersaline lake.";
RL Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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:RKQ35804.1}.
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DR EMBL; RBZP01000002; RKQ35804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495A872; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000269301; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000269301}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 390 AA; 42950 MW; 74CDA547ABF907E4 CRC64;
MNFELSEEIQ SLKEGIRDFI DKEVEPHAME IEETNEIPER IMEKSKQMGL FALSVPEEYG
GLGLSMVGKC AVLEEVGRTH NGFTTVIGGH TGIGGVGIVE MGTEKQKQKY LPGMASGERI
GAFALTEPAA GSHASNLKTT AVRKGDKYIL NGSKHYITNA PIADIFTVMA VTDPEKGARG
ITSFIVERDT PGLEIGKIEQ KMGLHGSHSS EVFFEDCEVP VENVLGEEGE GYVNALKILA
NGRAGMAARN LGSADKLLEM SLDYAHNRVQ FGKAIFEQQI IQHYLAEMAM EIEGLRSMVY
RVAAKVDRKE KVIKEAAMVK LLGSEVYNRV ADKAVQIHGG IGYISEYPIE RFYRDARITR
IYEGTSEIQK NIIAAQLHKE YEKRGVPHGV
//
