ID Q6NB70_RHOPA Unreviewed; 593 AA.
AC Q6NB70;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAE26402.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CAE26402.1};
GN OrderedLocusNames=RPA0958 {ECO:0000313|EMBL:CAE26402.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE26402.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE26402.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572596; CAE26402.1; -; Genomic_DNA.
DR RefSeq; WP_011156493.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6NB70; -.
DR STRING; 258594.RPA0958; -.
DR GeneID; 66891977; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_5; -.
DR PhylomeDB; Q6NB70; -.
DR Proteomes; UP000001426; 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; 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 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:UP000001426}.
FT DOMAIN 40..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 481..585
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 593 AA; 62131 MW; 3BB9895C10D8FBEC CRC64;
MTYRAPIDDI LLSLNHGAGL QAAVAAGHFG DYDSEITAQV LDEAGKFASD ILAPLNRVGD
KHGIKLEHGK VTTAPGWPDA YQRWIAAGWN AVSGPEDFGG QGLPMAVNAA CTEIWASSNM
AFGLCPLLTL SAIDALHTHG SDALKQVYLG KLISGEWTGT MQLTEPQAGS DVGALRTRAE
RAADGSYRIF GSKIFITYGD HDMTDNIVHF VLARLPDAPA GTKGISLFLV PKFLVNADGT
LGARNDIYPS GVEHKLGIHA SPTCTMTMGD HGGAIGYLIG EENRGMQCMF TMMNQARLAV
GLEGVGIADR AYQQALAYAQ ERKQGRAIGS AGPGSDPIIK HPDVKRTLLT MRALIGAART
ICYSTAVALD IAARSTDPKV KASAAARGAL LTPIAKAFST DIGIEVASLG VQIHGGMGFI
EETGAAQHYR DARIAPIYEG TNGIQAIDLV TRKLGANGGA SVFALLDELT LIVKDVEASN
DPGFGLTGLR LREGLEALDR TSRYLLDKLG SDTNDALAGA TPYLRLFGAT LGGCALAAEA
LAARDLEGIN DPSRYVALAR FFAETVAVQA PALERSVVDS AASVAGAEAV LTA
//
