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Database: UniProt
Entry: E8TFZ4_MESCW
LinkDB: E8TFZ4_MESCW
Original site: E8TFZ4_MESCW 
ID   E8TFZ4_MESCW            Unreviewed;       398 AA.
AC   E8TFZ4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE            EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN   OrderedLocusNames=Mesci_1983 {ECO:0000313|EMBL:ADV11136.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV11136.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) 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; CP002447; ADV11136.1; -; Genomic_DNA.
DR   RefSeq; WP_013529824.1; NC_014923.1.
DR   RefSeq; YP_004141186.1; NC_014923.1.
DR   AlphaFoldDB; E8TFZ4; -.
DR   STRING; 765698.Mesci_1983; -.
DR   KEGG; mci:Mesci_1983; -.
DR   PATRIC; fig|765698.3.peg.2438; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_8_0_5; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000007471; Chromosome.
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}.
FT   DOMAIN          21..133
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          137..232
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          245..390
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   398 AA;  43374 MW;  52E135F9CB265AB2 CRC64;
     MAADKNAFVW EDPFLIEGQL SEDERMVRDG AAAFAADRLA PRIEDAYLNE TFDTAIFREM
     GEAGLLGINI PEEFGGLGAN YVTYGLVARE VERVDSGYRS MMSVQSSLVM YPIYAYGSDE
     QRKKYLPKLA SGEWIGCFGL TEPDAGSDPG GMKTRAEKTA NGYKLSGSKM WISNAPVADV
     FVVWAKLKGE NGKDEIRGFV LEKGMKGLSA PKIGGKLSLR ASITGEVVME GVEVGEDALL
     PNAKGLGGPF GCLNRARFGI SWGSMGAAED CWHRARQYGL DRKQFGKPLA GTQLYQKKLA
     DMQTEIALGL QASLRVGRLL DEGKMAPEMI SIVKRNNCGK ALDIARQARD MHGGNGIQIG
     YHVMRHAQNL ETVNTYEGTH DVHALILGRA QTGLQAFF
//
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