ID K9YML7_CYASC Unreviewed; 585 AA.
AC K9YML7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AFZ47358.1};
GN OrderedLocusNames=Cyast_1394 {ECO:0000313|EMBL:AFZ47358.1};
OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ47358.1, ECO:0000313|Proteomes:UP000010483};
RN [1] {ECO:0000313|Proteomes:UP000010483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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|RuleBase:RU362125}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003940; AFZ47358.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YML7; -.
DR STRING; 292563.Cyast_1394; -.
DR KEGG; csn:Cyast_1394; -.
DR PATRIC; fig|292563.3.peg.1460; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_022921_0_0_3; -.
DR BioCyc; CSTA292563:G1353-1406-MONOMER; -.
DR Proteomes; UP000010483; 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF19; ACYL-COA DEHYDROGENASE FADE4-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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 Reference proteome {ECO:0000313|Proteomes:UP000010483}.
FT DOMAIN 124..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 585 AA; 66857 MW; 8DD1DC43C4FF614C CRC64;
MNPLPQYHTP EKLEQDLGNP IHGDSLMSYE KVIQIDESEQ FPHQEIDWLY QWNLQDYYIP
ENCGGKFTSF EEFIAIVRVL SRRDQTIGIA FTTLFWSFIT WMAGTQEQKD RLSEYIRNEH
GAMCLGYSEK DHGADLVGGE LTATKVDGGY VLNGEKWPIN RATISGMSYI LAKTADDNGG
RCLSLFMVEK SKINSENYYN LPKILTHGIR ASDMSGIGFK DCFVPDSMLI GKEGEGLEIA
LKGFQITRTL CSGFSHGAAD TALRTTLKFA LHRRVYEERV FDLPQPRKVL SDAFLDILIC
DCETIASCRG FHVVPEQFSV WSAVVKYFVT TQLETMINNI SAVLGSRFYM REEHDSGIFQ
KVLRDNAIIS VFDGSTVVNL HALILQFRQI TKTRQRLNEK RLRAIEENLK TIFSLDLKPP
TLQLDQLALF GKGADHVLQG LEIGLQKLAD LQNTYEVEPA VLKELIRLGD IVLLELNNHD
QTISQSNFEY GHHQSPETFE LAKKYCTLHT ATSCLFMWLY NRENLGEFFA KGEWLVLALN
RLLYAIRSIP YNIYEEYENN LSKEMVTLYK TEKVFSIVPF QLAKN
//
