ID Q8IAB6_CAEEL Unreviewed; 252 AA.
AC Q8IAB6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 149.
DE SubName: Full=Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000313|EMBL:CCD68092.1};
GN Name=acdh-1 {ECO:0000313|EMBL:CCD68092.1,
GN ECO:0000313|WormBase:C55B7.4b};
GN ORFNames=C55B7.4 {ECO:0000313|WormBase:C55B7.4b}, CELE_C55B7.4
GN {ECO:0000313|EMBL:CCD68092.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD68092.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD68092.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD68092.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284601; CCD68092.1; -; Genomic_DNA.
DR RefSeq; NP_871794.1; NM_181994.5.
DR AlphaFoldDB; Q8IAB6; -.
DR SMR; Q8IAB6; -.
DR IntAct; Q8IAB6; 1.
DR PeptideAtlas; Q8IAB6; -.
DR EnsemblMetazoa; C55B7.4b.1; C55B7.4b.1; WBGene00016943.
DR EnsemblMetazoa; C55B7.4b.2; C55B7.4b.2; WBGene00016943.
DR UCSC; C55B7.4b.4; c. elegans.
DR AGR; WB:WBGene00016943; -.
DR WormBase; C55B7.4b; CE32840; WBGene00016943; acdh-1.
DR GeneTree; ENSGT00970000196520; -.
DR HOGENOM; CLU_018204_7_2_1; -.
DR OrthoDB; 275353at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016943; Expressed in adult organism and 6 other cell types or tissues.
DR ExpressionAtlas; Q8IAB6; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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:SF5; ACYL COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:Q8IAB6,
KW ECO:0007829|PeptideAtlas:Q8IAB6};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 1..66
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 71..166
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 178..230
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 252 AA; 27562 MW; F50D17889CB8C22F CRC64;
MGVHVPEEYG GSGSSFFNAM IVIEELAKTD PSVSAMVGIH NTLPVSMIID YGTEEQKLKY
LPRLCSDSLA SFCISESGAG SDAFALKTIA KRDGDHFLIS GTKMWITNSG EAQVFVVFAN
ADPSQKYKGI TCFIVERSAD GLTVDKEEDK LGIRASSTCQ VHFDNVRVHK SAILGEYGKG
YKYAIECLNA GRIAIGAQMI GLAQGCFDQT IPYLQQREQF GQRLIDFQVI FEIGFEFLIH
KCSGFTTSDC TS
//