UniProt: A0A1S2L274

Database: UniProt
Entry: A0A1S2L274_9BACI

LinkDB:  A0A1S2L274_9BACI 
Original site:  A0A1S2L274_9BACI

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Ontology (2)   
   GO (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
Literature (2)   
   PubMed (2)   
All databases (21)   

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ID   A0A1S2L274_9BACI        Unreviewed;       380 AA.
AC   A0A1S2L274;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OIJ05917.1};
GN   ORFNames=AWH56_006465 {ECO:0000313|EMBL:QOY37269.1}, AWH56_21730
GN   {ECO:0000313|EMBL:OIJ05917.1};
OS   Anaerobacillus isosaccharinicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX   NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ05917.1, ECO:0000313|Proteomes:UP000180175};
RN   [1] {ECO:0000313|EMBL:OIJ05917.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:OIJ05917.1,
RC   ECO:0000313|Proteomes:UP000180175};
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT   Anaerobacillus genus.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QOY37269.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY37269.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=28104661;
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT   Anaerobacillus Genus.";
RL   Genome Announc. 5:e01493-16(2017).
RN   [3] {ECO:0000313|EMBL:QOY37269.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY37269.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=29580368;
RA   Bassil N.M., Lloyd J.R.;
RT   "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT   degrades isosaccharinic acid.";
RL   Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN   [4] {ECO:0000313|EMBL:QOY37269.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY37269.1};
RA   Bassil N.M., Lloyd J.R.;
RL   Submitted (OCT-2020) 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; LQXD01000187; OIJ05917.1; -; Genomic_DNA.
DR   EMBL; CP063356; QOY37269.1; -; Genomic_DNA.
DR   RefSeq; WP_071319019.1; NZ_CP063356.1.
DR   AlphaFoldDB; A0A1S2L274; -.
DR   KEGG; aia:AWH56_006465; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000180175; Chromosome.
DR   Proteomes; UP000180175; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 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; 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; 1.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000180175}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..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;  41357 MW;  66F48200672B4BAA CRC64;
     MELRFTEEQE MMRKMVRDFA QEQIAPMVAE MEETDRFPKE IIKQMGDLGL LGIPISEEYG
     GSDMDFTSYI IAIHELSKVS ATVGVILSVH TSVGTNPILY FGTEEQKQKY VPKLATGEYL
     GAFAITEPGA GSDAASIRTS AVKDGDHYVI NGSKIFITNA GEADTYIVSA KTDPSAGVKG
     ISVFIVEKDT PGFSVGKKEH KMGLHGSNTC ELIFEDVRVP VSNLLGEEGE GFKILMSNLD
     VGRIGIAAQS LGIAEAALES AIGYAKERQQ FGKPIGMQQG LGFKLADMAT KVEAAKLLVY
     RAAALRQKGL PCGQEASMAK LFASRAAMEV ATEAIQVFGG YGYTKDYPVE RYFRDAKICE
     IYEGTSEIQR IVISKHLLRD
//

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