ID B7P7P2_IXOSC Unreviewed; 410 AA.
AC B7P7P2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00044204};
DE EC=1.3.8.1 {ECO:0000256|ARBA:ARBA00012046};
DE AltName: Full=Butyryl-CoA dehydrogenase {ECO:0000256|ARBA:ARBA00031895};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW002863 {ECO:0000313|EMBL:EEC02614.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC02614.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC02614.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW002863-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW002863-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000256|ARBA:ARBA00001483};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000256|ARBA:ARBA00001483};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000256|ARBA:ARBA00023695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000256|ARBA:ARBA00023695};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.1;
CC Evidence={ECO:0000256|ARBA:ARBA00043785};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC Evidence={ECO:0000256|ARBA:ARBA00043785};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005198}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; ABJB010033668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010164820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010555520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010658223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010796583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010802303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011094510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011113437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS652836; EEC02614.1; -; Genomic_DNA.
DR RefSeq; XP_002399411.1; XM_002399370.1.
DR AlphaFoldDB; B7P7P2; -.
DR STRING; 6945.B7P7P2; -.
DR PaxDb; 6945-B7P7P2; -.
DR EnsemblMetazoa; ISCW002863-RA; ISCW002863-PA; ISCW002863.
DR KEGG; isc:IscW_ISCW002863; -.
DR VEuPathDB; VectorBase:ISCI002863; -.
DR VEuPathDB; VectorBase:ISCP_016631; -.
DR VEuPathDB; VectorBase:ISCW002863; -.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; B7P7P2; -.
DR OMA; LYREAPM; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046359; P:butyrate catabolic process; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd01158; SCAD_SBCAD; 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; 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; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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 PIRSF; PIRSF016578; HsaA; 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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 ECO:0000313|EMBL:EEC02614.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7P7P2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555}.
FT DOMAIN 33..144
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 148..243
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 255..403
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEC02614.1"
SQ SEQUENCE 410 AA; 44527 MW; 1D8A24EC75227A5A CRC64;
PSTGMTGALC DFCAGPIRTR WQCVRTLYAR LPDTHEMLQK TCREFAEKEL KPIAGTLDRE
HRYPREQIRR LGEMGLMAVA VPTELGGAGL DYLAYAIGME EISRGCASTG VVMSVNNSLF
LGAVLKYGSE AQKEKFIRPF TTGERVGCFA LSEPGNGSDA GAASTTAVLE GDHYRINGTK
AWITSAHEGE AAVVMATVDK SKKHKGISAF LVPMPTQGLT LGKKEEKLGI RASSTSYLIF
EDCLIPKEYR LGDEGMGFKI AMSVLDSGRI GIAGQALGIG QAALECALEY SGKRQSFGQS
LHSFQAIQMK LADMEVRLQS ARLLTWRAAM LKDAGLKFTK EAAMAKLAAS EAATYVSHQA
IQILGGMGYV TDMPAERHYR DARITEIYEG TSEVQRLVIA NNLLKEYGIV
//
