ID Q0RGH7_FRAAA Unreviewed; 409 AA.
AC Q0RGH7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Putative medium-chain Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAJ63410.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CAJ63410.1};
GN OrderedLocusNames=FRAAL4769 {ECO:0000313|EMBL:CAJ63410.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63410.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ63410.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ63410.1; -; Genomic_DNA.
DR RefSeq; WP_011605884.1; NC_008278.1.
DR AlphaFoldDB; Q0RGH7; -.
DR STRING; 326424.FRAAL4769; -.
DR KEGG; fal:FRAAL4769; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_1_0_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000000657; 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 CDD; cd00567; ACAD; 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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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.
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:CAJ63410.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT DOMAIN 9..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 130..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 242..388
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 409 AA; 44744 MW; E0030646A70FE47B CRC64;
MIDFSLPQEL VDLRERVRSF VENEIVPFER DPRLTAHGPT DELRQDLVGL ARKAGLLTIQ
APRRFGGREL THIEQAVVYE AAGWSTLGPV AMNCAAPDEA NMGLLAKIAD PEQQEEFLRP
VIEGGARSVF AMTEPGGAGS DPNQLLTEAV RDGDDFVVNG RKWLITGANG ALTWIIMARL
APGADGLGGP TLFLTRGDTP GIEVERVMNT MDRNYVEGHG VVTFRDLRLP ASAVLGTPGD
AFRYAQLRLT PARLTHCMRW LGAADRAHSI AVEHARTRTA FGRPIGEHQG VGFQLADNEI
ALDNCRLAIW HACWLLDRGE QGRHEASKVK CYVSEELFRV ADRCVQVLGG IGVTDETVVE
MIFRDIRAFR LYDGPTEVHK HAVARRLLRA RTTTPAVPAP AASGIPTPG
//
