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Database: UniProt
Entry: A0A086P4M6_SPHHM
LinkDB: A0A086P4M6_SPHHM
Original site: A0A086P4M6_SPHHM 
ID   A0A086P4M6_SPHHM        Unreviewed;       394 AA.
AC   A0A086P4M6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KFG88344.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:KFG88344.1};
GN   ORFNames=BV98_003927 {ECO:0000313|EMBL:KFG88344.1};
OS   Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 /
OS   MH) (Sphingomonas herbicidovorans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1219045 {ECO:0000313|EMBL:KFG88344.1, ECO:0000313|Proteomes:UP000024284};
RN   [1] {ECO:0000313|EMBL:KFG88344.1, ECO:0000313|Proteomes:UP000024284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16415 {ECO:0000313|EMBL:KFG88344.1,
RC   ECO:0000313|Proteomes:UP000024284};
RA   Gan H.M., Gan H.Y., Savka M.A.;
RT   "Draft genome sequences of Sphingobium herbicidovorans.";
RL   Submitted (AUG-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFG88344.1}.
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DR   EMBL; JFZA02000062; KFG88344.1; -; Genomic_DNA.
DR   RefSeq; WP_037469561.1; NZ_JFZA02000062.1.
DR   AlphaFoldDB; A0A086P4M6; -.
DR   STRING; 76947.GCA_002080435_03852; -.
DR   PATRIC; fig|1219045.3.peg.3987; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000024284; Unassembled WGS sequence.
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   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; 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   ECO:0000313|EMBL:KFG88344.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024284}.
FT   DOMAIN          7..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..203
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          239..386
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   394 AA;  42589 MW;  9864AF0EDB7303CF CRC64;
     MATAEKDDAR AIARRVEQFT RETIIPYETD GRRDDHGPLD TLVDEMRAKA REAGVLTPHI
     RADGSHLSHR DTAQVLRASG LSPLGPLACN TNAPDEGNMF LLGKVATPEQ KRAFLAPLHA
     GEGRSCFLMT EPAAEGGAGS DPSMMQTRAA LQDGEWVVNG RKAFATGFAG ATFAILMART
     DREDGAAGAT MFLVPLPHPA LVQERLIGTI DSSMPGGHAV VKIDNLRLPA SSILGAPHEG
     FAYAQIRLAP ARLTHCMRWL GAATRANEIA ADYAVKRQAF GKALIDHEGV GFMLADNLID
     LKQCELMIDW CADALDAGEM AITESSIAKV SVSETLFRVA DRCVQVMGGT GVSHDTIVEQ
     VFREIRAFRI YDGPTQVHKW SLAKKIKREA LARP
//
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