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Database: UniProt
Entry: A0Z5S5_9GAMM
LinkDB: A0Z5S5_9GAMM
Original site: A0Z5S5_9GAMM 
ID   A0Z5S5_9GAMM            Unreviewed;       416 AA.
AC   A0Z5S5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Probable acyl-CoA dehydrogenase {ECO:0000313|EMBL:EAW40685.1};
GN   ORFNames=MGP2080_13213 {ECO:0000313|EMBL:EAW40685.1};
OS   marine gamma proteobacterium HTCC2080.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW40685.1, ECO:0000313|Proteomes:UP000004719};
RN   [1] {ECO:0000313|EMBL:EAW40685.1, ECO:0000313|Proteomes:UP000004719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW40685.1,
RC   ECO:0000313|Proteomes:UP000004719};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
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:EAW40685.1}.
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DR   EMBL; AAVV01000007; EAW40685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Z5S5; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000004719; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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   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:UP000004719}.
FT   DOMAIN          25..138
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          143..237
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          249..413
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   416 AA;  45478 MW;  36E91A192B6BED7B CRC64;
     MSACEARARI CRRHKQIEGS VMTDYQIFRK SVKDFLGEAL TPELRRAGEL TTSVFSEFSA
     ALAWQKKLHA QGWIAPDWPS EFGGPGWDIQ QRSIFQEECK LANAPSVVMM GIQMLGPMLM
     HYGTEEQKQY YLPRMLSGAD IWCQGYSEPG AGSDLASLKT TAVRDGDNYV VNGTKIWTSM
     AHHANQIFCL VRTDKAVKPQ AGISFLLIDL ESPGITITPI VSLDGQVEQC QVFFDAVKVP
     CANLVGAEND GWSVAKSLLE FERGGHNFTI DVKKQLRKIH SQAKLTPWGE KTRAADPVFQ
     HRLAEAEIDA LALEHTELRI KGAVEAGGNP GALSSLVKVV GTELGQRLNE LSIDLVGPAA
     APQCLEALDP NHKGDTPVPE HALTAMAEYI NNRAATIYGG TAEIQRTIIA KKVLGL
//
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