ID A0A2N5GUB8_9BACI Unreviewed; 385 AA.
AC A0A2N5GUB8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PLR91608.1};
GN ORFNames=CVD19_21745 {ECO:0000313|EMBL:PLR91608.1};
OS Bacillus sp. T33-2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2054168 {ECO:0000313|EMBL:PLR91608.1, ECO:0000313|Proteomes:UP000235118};
RN [1] {ECO:0000313|EMBL:PLR91608.1, ECO:0000313|Proteomes:UP000235118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T33-2 {ECO:0000313|EMBL:PLR91608.1,
RC ECO:0000313|Proteomes:UP000235118};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-2017) 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:PLR91608.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGVB01000041; PLR91608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5GUB8; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000235118; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000235118}.
FT DOMAIN 8..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 232..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 385 AA; 43052 MW; DDEEBD0DC568CD31 CRC64;
MAYEPYFTEE HEQLRKTVRK FVEKEVTPYV DDWEEKGEFP LEIFRRMGDL GFLGLRYPEN
AGGQGWDYFA GIVFAEEMAK CGCGGFPMAV AVQTDMATPP IMEFGNDEQI ERFLKPALKG
EKLAAIGISE PNHGSDVASI ETRARLEGNE WVINGSKTFI TNGPRADFIT LVARTNEKPG
HKGISLILVE LDRPGVSISR KLDKVGMRSS DTAEIIFDNV TVPYDNLLGK EGQGFAQIMW
ELQGERMISA AGSIGIAECA YEHALQYAKT RNQFGTPIAG FQVISHLLAE MKTEIELCKE
MTYATAYRFS QGEVPSKEIS MVKLAAARMA HWVADRALQV FAGSGYMMEN PIQRIWRDTR
LYRIGAGTDE IMKEIISKQM GLETV
//