ID A9CGL8_AGRFC Unreviewed; 395 AA.
AC A9CGL8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN Name=gcdH {ECO:0000313|EMBL:AAK89022.1};
GN OrderedLocusNames=Atu4418 {ECO:0000313|EMBL:AAK89022.1};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK89022.1, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK89022.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK89022.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007870; AAK89022.1; -; Genomic_DNA.
DR PIR; AF3099; AF3099.
DR PIR; D98187; D98187.
DR RefSeq; NP_356237.1; NC_003063.2.
DR RefSeq; WP_010973831.1; NC_003063.2.
DR AlphaFoldDB; A9CGL8; -.
DR STRING; 176299.Atu4418; -.
DR EnsemblBacteria; AAK89022; AAK89022; Atu4418.
DR KEGG; atu:Atu4418; -.
DR PATRIC; fig|176299.10.peg.4225; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_8_0_5; -.
DR OrthoDB; 9775090at2; -.
DR PhylomeDB; A9CGL8; -.
DR BioCyc; AGRO:ATU4418-MONOMER; -.
DR Proteomes; UP000000813; Chromosome linear.
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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000000813}.
FT DOMAIN 20..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 136..229
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 243..387
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 395 AA; 43543 MW; E164B9CBCA7FAD83 CRC64;
MSERAAFHWQ DPFLLEDQLT DDERMIRDSA EAFGKSELLP RISEAYLSET TEPELFRLMG
RTGLLGVTLP EEYGAANASY VAYGLVAREV ERIDSGYRSM MSVQSSLVIH PIFAYGSDEQ
KKKYLPGLVS GELIGCFGLT EPDAGSDPGG MKTRAEKIEG GYRLRGSKMW ISNAPIADVF
VVWAKSEAHD NEIRGFVLEK GMKGLSAPKI GGKLSLRASI TGEIVMDGVE VGEDALLPNV
SGLKGPFGCL NRARYGISWG VMGAAEDCWF RSRQYGLDRK QFGKPLAGTQ LYQKKLADMQ
TEIALGLQAS LRVGRLMDEH KMAPEMISIV KRNNCGKALD IARQARDMHG GNGIQIEYHV
MRHAQNLETV NTYEGTHDVH ALILGRAQTG IQAFF
//
