ID A0A432WGP1_9GAMM Unreviewed; 592 AA.
AC A0A432WGP1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RUO32970.1};
GN ORFNames=CWE14_06905 {ECO:0000313|EMBL:RUO32970.1};
OS Aliidiomarina soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=1928574 {ECO:0000313|EMBL:RUO32970.1, ECO:0000313|Proteomes:UP000287823};
RN [1] {ECO:0000313|EMBL:RUO32970.1, ECO:0000313|Proteomes:UP000287823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y4G10-17 {ECO:0000313|EMBL:RUO32970.1,
RC ECO:0000313|Proteomes:UP000287823};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO32970.1}.
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DR EMBL; PIPO01000003; RUO32970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432WGP1; -.
DR Proteomes; UP000287823; 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:UP000287823}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 39..159
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..273
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 468..584
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 592 AA; 63774 MW; A84E2FDC80EE7521 CRC64;
MSDYKASLQD MNFVLHEVFG VADDWAVMPE LQEMMDADTA TAILEEAAKV TEGLIAPNAR
NADEQGVSYR DATVTTPDGY KEAFRQLAEG GWVGVTANPE LGGMGLPKVI SAQYEEMMCA
ADISFSLYSG LTAGAIIALD SHASDEIKQT YIPRMAAGEW TGTMCLTEPH AGTDLGIIRT
KAEPQADGSF ALSGTKIFIT GGEHDLTDNI IHLVLAKLPD ALAGSKGISL FIVPKFLVND
DGSLGERNAV AAGSVEHKMG IHGSATCVMN FDGAKGWLVG EPNRGLAAMF TMMNYERLGV
GIQGLGAAAR SYGTALDYAK DRRQGRGAKA TQDTSASADT LLVHGDIRRM LLTMKAFIEG
GRAFSSYVGQ QLDRAKYAPH VEEREAADKL VALLTPVAKA FMTDTGLEAT IHGQQILGGH
GYVREWGQEQ WVRDCRIAQI YEGTNGIQAL DLLGRKVAGS RGELLKPLLA DIEKTLNEAG
DNWSKEAAQL RAATEALVSV TEGILKQVPT DENIINSLAV EYLQLVGYVA YAYLWLRMAL
VAEASDSTDS FYSAKVKTAR FYFAKLLPRI DGLVGALESG SESLYLHDED DF
//
