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Database: UniProt
Entry: K7AB29_9ALTE
LinkDB: K7AB29_9ALTE
Original site: K7AB29_9ALTE 
ID   K7AB29_9ALTE            Unreviewed;       373 AA.
AC   K7AB29;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AGH42364.1};
GN   ORFNames=C427_0254 {ECO:0000313|EMBL:AGH42364.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH42364.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH42364.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH42364.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(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}.
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DR   EMBL; CP003837; AGH42364.1; -; Genomic_DNA.
DR   RefSeq; WP_007638271.1; NZ_BAES01000046.1.
DR   AlphaFoldDB; K7AB29; -.
DR   STRING; 1129794.C427_0254; -.
DR   KEGG; gps:C427_0254; -.
DR   PATRIC; fig|1129794.4.peg.250; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_5_2_6; -.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000011864; 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   CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF44; BLR1022 PROTEIN; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT   DOMAIN          7..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..214
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..369
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   373 AA;  40583 MW;  6E5BC9FE40B89DD6 CRC64;
     MDFSLSSEQK MIQDSVSRFV LNDYDFDTRR KILGSTTGYS QENWNVFAEL GWLMLPFSEE
     DGGLSGSMVD LALVMEEFGK GMVVEPFIAT TVMAGGLVAL AGNQQQKDDY LPKIMAGELQ
     MAFAYAESQS RYNLNNVKCS ANKIDGEFVI TGQKSVVLNG NHADTLIVAA RTSGDTNDTH
     GISLFLVDAK HASVTRQGYA NVDGHQAADI SFDNTPTLGL LGELDIALPA INNIIDRATL
     AICAEAVGAM QIAHERTLEY AKTRKQFGRT IGSFQALQHR MVNMFIEHQQ AKSILLMAAL
     KMDSNNGSDA KALSAAKSRI GKAASLVGRE SIQIHGGIGM TDEIDVGHIF KRLTTIQFLF
     GSTDVHTRRF ASL
//
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