(data stored in ACNUC7421 zone)

SWISSPROT: A1AYH0_PARDP

ID   A1AYH0_PARDP            Unreviewed;       386 AA.
AC   A1AYH0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ABL68314.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:ABL68314.1};
GN   OrderedLocusNames=Pden_0198 {ECO:0000313|EMBL:ABL68314.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68314.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000489; ABL68314.1; -; Genomic_DNA.
DR   RefSeq; WP_011746547.1; NC_008686.1.
DR   STRING; 318586.Pden_0198; -.
DR   PRIDE; A1AYH0; -.
DR   EnsemblBacteria; ABL68314; ABL68314; Pden_0198.
DR   KEGG; pde:Pden_0198; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   KO; K06446; -.
DR   OMA; MCDVHNT; -.
DR   BioCyc; PDEN318586:G1GW1-196-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
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.
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; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AYH0.
DR   SWISS-2DPAGE; A1AYH0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:ABL68314.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN        6    117       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      121    217       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      232    380       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   386 AA;  41746 MW;  76E4D71AD9FA5880 CRC64;
     MSLDPETLAQ FLETLDRFVR ERLIPNEERV ADGDAIPPEL VQEIREMGLF GMSIPEEHGG
     IGLTMAEEVQ AALVLGQASP VFRSLVGTNN GIGSQGIIID GTPEQKAHYL PQLASGEMIA
     SFALTEPDAG SDAGSLRCSA RLDGDHYVLN GTKRFITNAP HAGLFTVFAR TDPDSKSAAG
     VTAFLVEAGT PGLHLGPRDR KMGQKGSHTC DVILEDCRVP ASAIIGGPDR LGQGFKTAMK
     VLDRGRLHIS AVCVGAAERL IRDSLAYAME RRQFGEPIAE KQLVQAMLAD SRAEAYAARC
     MIEETARRKD AGLSVSTEAA CCKMYASEMV GRVADRAVQI HGGAGYMAEY AVERFYRDVR
     LFRIYEGTTQ IQQLVIARNM IREASG
//

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