UniProt: A0A0A1DM83

Database: UniProt
Entry: A0A0A1DM83_NOCSI

LinkDB:  A0A0A1DM83_NOCSI 
Original site:  A0A0A1DM83_NOCSI

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   A0A0A1DM83_NOCSI        Unreviewed;       389 AA.
AC   A0A0A1DM83;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GEB16240.1};
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AIY18464.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:AIY18464.1};
GN   ORFNames=KR76_19950 {ECO:0000313|EMBL:AIY18464.1}, NSI01_45550
GN   {ECO:0000313|EMBL:GEB16240.1};
OS   Nocardioides simplex (Arthrobacter simplex).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Pimelobacter.
OX   NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY18464.1, ECO:0000313|Proteomes:UP000030300};
RN   [1] {ECO:0000313|EMBL:AIY18464.1, ECO:0000313|Proteomes:UP000030300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY18464.1,
RC   ECO:0000313|Proteomes:UP000030300};
RX   PubMed=25573942;
RA   Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA   Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT   Ac-2033D.";
RL   Genome Announc. 3:0-0(2015).
RN   [2] {ECO:0000313|EMBL:GEB16240.1, ECO:0000313|Proteomes:UP000318936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB16240.1,
RC   ECO:0000313|Proteomes:UP000318936};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL   Submitted (JUN-2019) 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; CP009896; AIY18464.1; -; Genomic_DNA.
DR   EMBL; BJMC01000022; GEB16240.1; -; Genomic_DNA.
DR   RefSeq; WP_038680722.1; NZ_JAAARG010000448.1.
DR   AlphaFoldDB; A0A0A1DM83; -.
DR   STRING; 2045.KR76_19950; -.
DR   KEGG; psim:KR76_19950; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   OrthoDB; 142556at2; -.
DR   Proteomes; UP000030300; Chromosome.
DR   Proteomes; UP000318936; 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   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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   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; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT   DOMAIN          10..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..382
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   389 AA;  41737 MW;  DDF6632059BDEE7B CRC64;
     MSDFPMYALS EEHQAIREAV RAICDAKVAP FAAAVDEEAR YPHEAAAALR AADFHAPHVP
     EEFGGAGADA LATVLVIEEV ARADVSASLI PAVNKLGSLP VMIGGSEELK KHYLGALARG
     EGGFSYCLSE PDAGSDAANQ KTRAVRDGDD WILNGTKRWI SNAGESEFYT VLATTDPDAR
     TKGISAFVVE KSDAGVSFGA PEKKLGIKGS PTREVYLDNV RIPGDRIIGE EGKGFEYAMK
     TLDHTRITIA AQAVGVAQGA LDYALSYAKE RQQFGKSIAD FQGLQFLLAD MGMKVEAARQ
     LTYAAAGRSE RGDSDLTFFG AAAKCFASDV AMEVTTNAVQ VLGGYGYTRD YPVERMMRDA
     KITQIYEGTN QVQRIVMARQ LLAGVQSEI
//

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