ID Q2KCR1_RHIEC Unreviewed; 598 AA.
AC Q2KCR1;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Acyl-CoA dehydrogenase protein {ECO:0000313|EMBL:ABC89375.1};
GN Name=acd1 {ECO:0000313|EMBL:ABC89375.1};
GN OrderedLocusNames=RHE_CH00557 {ECO:0000313|EMBL:ABC89375.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC89375.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC89375.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP000133; ABC89375.1; -; Genomic_DNA.
DR RefSeq; WP_011423926.1; NC_007761.1.
DR AlphaFoldDB; Q2KCR1; -.
DR KEGG; ret:RHE_CH00557; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_5; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936}.
FT DOMAIN 4..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 80..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 467..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 598 AA; 64980 MW; 2A2928FD6864E734 CRC64;
MPVYKAPVND TLFVLNDVLG LERYNNLPGF ADATPDMIEA ILGEAAKVAE EVLFPVNYSG
DQEGCRRQDD ASVSTPKGFK EAYNAYREGG WIGLAVPEEF GGQGLPYTLH TAVGEYTSAA
NMSLMMYPGL TQGAIAAILV HGTQEQKETY LPKMVDGSWS GTMNLTEPHC GTDLGMLRTR
AVPQADGSYK ISGQKIFISA GEHDLTDNIV HLVLARIEGA PEGTKGISLF IVPKFLVGKD
GALGARNAVT CGAIEHKMGI HGNATCVMNY DEATGFLIGA ENRGLNAMFV MMNEARLMVG
LQGIAISEIA YQNAANYARD RIQGRSLSGV KAPDKKADPI IVHPDIRRSL MTIRAFNEAG
RAFLLWTALK SDIAHRATDE KERQTADDIL GLVTPILKGV MTDRGFDHAV MAQQVFGGHG
YIEEHGMSQY VRDARIAMIY EGANGIQALD LVGRKLALNG GRAAMALFKE IGDFCEENRS
DEKLSFFTRH LKKGLNDVQG ATMWFMQNAM AKPDNAGAGS TDYMHLFGLV VLGYMWAKMA
KAAEDGLASG DASREDYLKN KLITAKFFME RIMPETALRK ARIEAGADTM MALAAEAF
//
