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Database: UniProt
Entry: S8B674_PENO1
LinkDB: S8B674_PENO1
Original site: S8B674_PENO1 
ID   S8B674_PENO1            Unreviewed;       446 AA.
AC   S8B674;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PDE_09342 {ECO:0000313|EMBL:EPS34378.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34378.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS34378.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; KB644415; EPS34378.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8B674; -.
DR   STRING; 933388.S8B674; -.
DR   eggNOG; KOG1469; Eukaryota.
DR   HOGENOM; CLU_018204_1_2_1; -.
DR   OrthoDB; 276350at2759; -.
DR   PhylomeDB; S8B674; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   DOMAIN          17..142
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          146..248
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          260..411
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   446 AA;  49138 MW;  069F1C090132C852 CRC64;
     MSASTRIPVI AQPFVSERAK KTLDLVEEFV EKECIPAEAV FSAQLGEGEK RWQTTPAVME
     ELKAKAKKLG LWNMFLAKSH FKEGAGYSNV EYGLMAEILG KSKVASEATN NAAPDTGNME
     VLAKYGNEAQ KKEWLAPLLE GKIRSAFLMT EPDVASSDAT NIELEIRREG NEYVLNGSKW
     WSSGAGDPRC KVYLVMGKSD PKNTDTYRQQ SVVLCPADAP GVTVHRMLHV YGYDDAPHGH
     GHITFKNVRL PLSSMVLGEG RGFEIIQGRL GPGRIHHAMR TIGAAEKALE WMIARVNDER
     KKTFGKALSS HGVILEWIAK SRIEVDAARL IVLNAAIKID QGDAKAALKE IAEAKVLVPQ
     SALAIIDRAV QAYGAAGVCQ DTPLAYMWAG IRTLRIADGP DEVHLQQMGR RENESRKKEV
     IAKLKWQQQE SDRLLIASGF KAKSHL
//
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