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Database: UniProt
Entry: Q2GA20_NOVAD
LinkDB: Q2GA20_NOVAD
Original site: Q2GA20_NOVAD 
ID   Q2GA20_NOVAD            Unreviewed;       380 AA.
AC   Q2GA20;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ABD25303.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:ABD25303.1};
GN   OrderedLocusNames=Saro_0858 {ECO:0000313|EMBL:ABD25303.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD25303.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000248; ABD25303.1; -; Genomic_DNA.
DR   RefSeq; WP_011444517.1; NC_007794.1.
DR   AlphaFoldDB; Q2GA20; -.
DR   STRING; 279238.Saro_0858; -.
DR   KEGG; nar:Saro_0858; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_5; -.
DR   Proteomes; UP000009134; Chromosome.
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; 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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:ABD25303.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT   DOMAIN          8..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          124..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41085 MW;  4D49F72E1C25D828 CRC64;
     MTEQFALTED QIAIQDMARR FTADAITPFA AQWDEDHTFP RDTIKAAAEL GFAAIYVSEE
     SGGIGLGRLE AALIMEAMAY GCPATSAFIS IHNMAAWMID KFGGDEIKSR YLPSLVTMDQ
     IASYCLTEPG SGSDAAALKT TARLEGDHYV VNGTKQFISG GGVNDLYVTM VRTGDNGAKG
     ISCLVIEKDM PGVSFGAPER KLGWNASPTA QVIFDNVKVP VANRVGAEGD GFKFAMAGLD
     GGRLNIGACS LGGAQRCLDE AVAYVKDRSQ FGKAIAEFQN TQFQLADMAT DLEASRALLY
     LAAAKVTANA PDKTRFSAMA KKLATDNGSS IVDRALQMFG GYGYLRDYPI ERFWRDLRVH
     RILEGTNEVM RMIVGRDLLK
//
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