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Database: UniProt
Entry: A0A0U1NIV2_9RHOB
LinkDB: A0A0U1NIV2_9RHOB
Original site: A0A0U1NIV2_9RHOB 
ID   A0A0U1NIV2_9RHOB        Unreviewed;       412 AA.
AC   A0A0U1NIV2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE            EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN   Name=acdA {ECO:0000313|EMBL:CRK74657.1};
GN   ORFNames=NIG5292_00692 {ECO:0000313|EMBL:CRK74657.1};
OS   Nereida ignava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Nereida.
OX   NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74657.1, ECO:0000313|Proteomes:UP000048949};
RN   [1] {ECO:0000313|EMBL:CRK74657.1, ECO:0000313|Proteomes:UP000048949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74657.1,
RC   ECO:0000313|Proteomes:UP000048949};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036548};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC       {ECO:0000256|ARBA:ARBA00037899}.
CC   -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC       {ECO:0000256|ARBA:ARBA00037927}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CVQV01000003; CRK74657.1; -; Genomic_DNA.
DR   RefSeq; WP_048598000.1; NZ_CVQV01000003.1.
DR   AlphaFoldDB; A0A0U1NIV2; -.
DR   STRING; 282199.GCA_001049735_00692; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000048949; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01151; GCD; 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; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42807:SF1; GLUTARYL-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   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   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   ECO:0000313|EMBL:CRK74657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048949}.
FT   DOMAIN          37..148
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          153..246
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          259..404
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   412 AA;  44292 MW;  1DA3A13C4F197DFC CRC64;
     MNAQHPVDPI QSHPAGHGPE LSRFDWAEPF LLNAQLTEEE RMLAEAAETF SQNALAPLVT
     DSYRDESFDR SLFEKMGSAG LLGATIPESY GGLGAGYVSY GLIARAVERV DSGYRSMMSV
     QSSLVMYPIF AYGTEEQRQK YLPGLAAGTS IGCFGLTEPD AGSDPAGMKT TAVKTPTGYR
     LNGAKMWISN APAADVFVVW AKSEAHGGKI RGFVLDKGTK GLSAPVIKGK LSLRASITGE
     IVMSDVDVGE DALLPNVEGL KGPFGCLNRA RYGISWGVMG AAEACWHAAR QYGLDRHQFG
     KPLAQTQLFQ KKLADMQTEI ALGLQGSLQL GRMMDGGSAS PELISMMKRN NCGKALDVAR
     HARDMHGGNG ISDAFPVMRH MVNLETVNTY EGTHDIHALI LGRAQTGLQA FF
//
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