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Database: UniProt
Entry: A0A017HTP5_9RHOB
LinkDB: A0A017HTP5_9RHOB
Original site: A0A017HTP5_9RHOB 
ID   A0A017HTP5_9RHOB        Unreviewed;       409 AA.
AC   A0A017HTP5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE            EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN   ORFNames=Rumeso_00871 {ECO:0000313|EMBL:EYD77705.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD77705.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD77705.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD77705.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYD77705.1}.
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DR   EMBL; AOSK01000024; EYD77705.1; -; Genomic_DNA.
DR   RefSeq; WP_037281766.1; NZ_KK088593.1.
DR   AlphaFoldDB; A0A017HTP5; -.
DR   STRING; 442562.Rumeso_00871; -.
DR   PATRIC; fig|442562.3.peg.865; -.
DR   HOGENOM; CLU_018204_8_0_5; -.
DR   Proteomes; UP000019666; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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:EYD77705.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019666}.
FT   DOMAIN          34..146
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          150..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          256..401
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   409 AA;  43864 MW;  A8D3F844D2274DEC CRC64;
     MNEATRITAD STGHGPGLSA FDWADPLRLE DQLTEDERML RDAARQFAES RLAPRVREAY
     HEETADPSIF REMGEAGLLG VTIPEEHGGL GAGYVSYGLV AREVERVDSG YRSMMSVQSS
     LVMYPIHAYG SDAHRARYLP GLASGELIGC FGLTEPDAGS DPGGMRTTAR RTAGGYLLNG
     TKTWISNAPL ADVFVVWAKS EAHGGKIRGF VLDKGANGLS APKIGGKLSL RASVTGQIVM
     EDVEVPEDAL LPGVEGLKGP FGCLNRARFG ISWGVMGAAE ACWHTARQYG LDRKQFGKPL
     AANQLFQRKL ADMQTEIALG LQGALALGRM MEAGTASPEA ISLMKRNNCG KALDVARASR
     DMLGGNGISD AFPVMRHMIN LETVNTYEGT HDVHALILGR AQTGLQAFQ
//
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