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Database: UniProt
Entry: A0A132MK98_9ACTN
LinkDB: A0A132MK98_9ACTN
Original site: A0A132MK98_9ACTN 
ID   A0A132MK98_9ACTN        Unreviewed;       610 AA.
AC   A0A132MK98;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KWW97811.1};
GN   ORFNames=LI90_86 {ECO:0000313|EMBL:KWW98466.1}, TH66_20430
GN   {ECO:0000313|EMBL:KWW97811.1}, TR74_07605
GN   {ECO:0000313|EMBL:KWX09771.1};
OS   Carbonactinospora thermoautotrophica.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Carbonactinosporaceae; Carbonactinospora.
OX   NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW97811.1, ECO:0000313|Proteomes:UP000070659};
RN   [1] {ECO:0000313|EMBL:KWW97811.1, ECO:0000313|Proteomes:UP000070659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBT1 {ECO:0000313|EMBL:KWW97811.1,
RC   ECO:0000313|Proteomes:UP000070659};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000070598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBT1 {ECO:0000313|Proteomes:UP000070598};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KWW98466.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|EMBL:KWW98466.1};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Woodward J., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000070188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA   Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) 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:KWW97811.1}.
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DR   EMBL; JYIJ01000019; KWW97811.1; -; Genomic_DNA.
DR   EMBL; LAXD01000001; KWW98466.1; -; Genomic_DNA.
DR   EMBL; JYIK01000726; KWX09771.1; -; Genomic_DNA.
DR   RefSeq; WP_066883209.1; NZ_PQID01000007.1.
DR   AlphaFoldDB; A0A132MK98; -.
DR   STRING; 1469144.LI90_86; -.
DR   PATRIC; fig|1469144.10.peg.156; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000070188; Unassembled WGS sequence.
DR   Proteomes; UP000070598; Unassembled WGS sequence.
DR   Proteomes; UP000070659; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070188}.
FT   DOMAIN          3..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          162..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          286..453
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          473..605
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   610 AA;  67898 MW;  7F6A1703F63F97B2 CRC64;
     MGHYKSNLRD LEFNLFEVFG RQEVLGKAPY AEVDVDTARS ILSEVERLAT NELADSLLDS
     DRNPPVFDPK THTAPLPESF KKSYQAWVNA EWWRLDLPEE LGGTVVPPSL RWAVQELVLG
     ANPAIHMYCS GPSFAHVIWR LGTEEQRKIA RQMVEKQWGA TMVLTEPDAG SDVGAGRTRA
     TQQPDGTWHI EGVKRFITSG EHDLADNIIH FVLARPDGAG PGTKGLSLFL VPKYLFDWDT
     GELKERNGVY ATNVEKKMGL KVSNTCEMTF GADRPAVGYL LGEVHDGIRQ MFMIIEFARM
     MVGTKAIATL STGYLNALEF AKTRVQGPDL TRMTDKTAPK VTIIHHPEVR RSLMLQKAYA
     EALRALYLYT ACVQDDAWSA TLQGKVDEDA ERYNDLLLPI VKGFGSEKSY ALLADALQIF
     GGSGYLQDYP LEQYIRDAKI DTLYEGTTAI QSMDLFFRKI VRDKGQALMR LNNEIQSFIN
     AGGESGDDFA EERRLLAKAL EDVQGIVGAM VGQLTSAGED PKNIYKVGQN TVRLLMCMGD
     LICGWLLLRQ AEVAKAKLAE GPSERDEHFY QGKIAAARFF ARTVLPTITP QRRIAESIDN
     ALMEVAEAAF
//
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