ID K6YYR8_9ALTE Unreviewed; 399 AA.
AC K6YYR8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AGH42365.1};
GN ORFNames=C427_0255 {ECO:0000313|EMBL:AGH42365.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH42365.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH42365.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH42365.1,
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; AGH42365.1; -; Genomic_DNA.
DR RefSeq; WP_007638273.1; NZ_BAES01000046.1.
DR AlphaFoldDB; K6YYR8; -.
DR STRING; 1129794.C427_0255; -.
DR KEGG; gps:C427_0255; -.
DR PATRIC; fig|1129794.4.peg.251; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_0_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 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:UP000011864}.
FT DOMAIN 6..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 232..397
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 399 AA; 44411 MW; D6C0E7F98B5B3C09 CRC64;
MNSNFTAEEK DFQQEVQQFL QEKLPKETAR KTKSALHLSK EECVEWQKIL HKQGWAATNW
PLEHGGTGWT QTQKYIFANE CAKAGGPDVI PFGLKMVAPI IYTFGNEEQK QRFLPDILAS
NVWWCQGYSE TGAGSDLAGV RTTAVKDGDE YVVNGTKTWT TLGQHADWIF CLVRTGPPSA
KNQEAISFLL INMHDPKIKV SPIITIDGRH EVNEVHFDEV RVPANNLIGT EGQGWTYAKV
LLTHERTGIA RVAISKDRLV QLKELVATSP NGEDKLMDDV IFAQKIANVE IDLLALEYTE
LRTLSAISTG QAPGPESSIL KIVGTQIIQA IDELYVEAAG YYSMPFVPYQ FYDDYDGAQI
GPDMATNSSL RYFNNRKTSI YGGSNEIQTN IISKAVLGL
//
