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Database: UniProt
Entry: A0A061H5B4_9BASI
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ID   A0A061H5B4_9BASI        Unreviewed;       461 AA.
AC   A0A061H5B4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFL1_04772 {ECO:0000313|EMBL:EPQ27634.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27634.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27634.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27634.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(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|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; KE361638; EPQ27634.1; -; Genomic_DNA.
DR   RefSeq; XP_007880491.1; XM_007882300.1.
DR   AlphaFoldDB; A0A061H5B4; -.
DR   GeneID; 19318872; -.
DR   KEGG; pfp:PFL1_04772; -.
DR   eggNOG; KOG1469; Eukaryota.
DR   HOGENOM; CLU_018204_1_2_1; -.
DR   OrthoDB; 276350at2759; -.
DR   Proteomes; UP000053664; 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:UP000053664}.
FT   DOMAIN          66..160
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          164..266
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          278..428
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   461 AA;  51034 MW;  6498F5FBB4478473 CRC64;
     MSLTTGPLTG DALITKYISP ATWALVQDKF SPFGKQTLIK VINFVEHECN PAEELYHAQV
     STDPATRWKI VPEIVEQLKK KAKAQGLWNL FLSKKHYPDV GTPLTNLEYG MMAEIMGRGS
     HFTSESMNCS APDTGNMEVF AKYGNQEQKD TWLRPLMNGE IRSAFAMTER FVASSDATNI
     RTSIRREGDE IVVNGHKWWI SGAGDPRCAV HLVMGKSDPD NANTHKQQSL VIVPANAPGV
     KVIRPMQVFG YDDAPEGHCE VIYDNVRVPL KNLVLDWGRG FEIIQGRLGP GRIHHCMRSI
     GTAERALDLL LMRATDQRKK AFGKTLSEHG VIVQNVAWCR IKIDQARLLV LSAANMIDAT
     NAKGALKDIA MSKVAVVKSA LEVVDMAMQA HGAEGVCQDT PLASAWAGLR TLRYADGPDE
     VHLQQLGKLE LRRAPELWDK ANLRSAVSKK LMDKHGLKSH L
//
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