ID K7A753_9ALTE Unreviewed; 601 AA.
AC K7A753;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AGH44058.1};
GN ORFNames=C427_1949 {ECO:0000313|EMBL:AGH44058.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH44058.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH44058.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH44058.1,
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|RuleBase:RU362125}.
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DR EMBL; CP003837; AGH44058.1; -; Genomic_DNA.
DR RefSeq; WP_007636164.1; NZ_BAES01000022.1.
DR AlphaFoldDB; K7A753; -.
DR STRING; 1129794.C427_1949; -.
DR KEGG; gps:C427_1949; -.
DR PATRIC; fig|1129794.4.peg.1930; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_6; -.
DR OrthoDB; 9807883at2; -.
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; 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; 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:SF3; ACYL-COA DEHYDROGENASE-RELATED; 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; 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT DOMAIN 5..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 162..234
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 468..594
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 601 AA; 66339 MW; 8D53A4539C771373 CRC64;
MPAPILSRRD IEFFLYEMFD VESLTTRERY QDHDRESFDA AIDIAQAIAE KYYVPIRLKV
DSNQPTFDGK KVHIIPEIKE GLDAVIEAGL TAPTTDYAMG GMQLPQIAAS GASAYIAAAA
STSIGYLSLT HANSNLIEAY GTPEQINKWV TPQRQGRFFG TMAMTEPGAG SGLGDLTTSA
TKEEDGTYRV KGNKIWISGG DHDLSENIVH LVLARVKGAP KGVKGISLFI VPKYLVGDDG
KIGDRNEVAL AGLFHKMGGR GQTSTALSFG EQNGAEAYLV GEENKGLMYM FHMMNEARIL
VGTGAALTAL TGFQYSLDYA KGRPQGRLLS AKDPLAPPVN IIEHPDVRRM LLTQKAYSEG
AYALCLYGHQ LSEDEKTAPT ESERKHASTI LDFLTPIIKS WPSEWGPKSN DLAIQVLGGH
GYVNEHPVEM FYRDNRLNPI HEGTTGIQSL DLLCRKVPMN DFKGYQAFLA EIQLTAESVK
LTESLQTYAV ALQHAVDNLK EVTTSVMGAS KTQNLDLVFS NSVSYLNMFG HLTIAWLWLR
QAEIATKQLG KAPHSDDEKF YHGKIQAMKY FFNSELPLTY HWGNLVKNID SASFDTHPDW
L
//
