ID K5BGZ9_MYCHD Unreviewed; 375 AA.
AC K5BGZ9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acyl-CoA dehydrogenase fadE12 {ECO:0000313|EMBL:VCT89111.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:VCT89111.1};
DE SubName: Full=Acyl-CoA dehydrogenase, N-terminal domain protein {ECO:0000313|EMBL:EKF24451.1};
GN ORFNames=C731_1520 {ECO:0000313|EMBL:EKF24451.1}, MHAS_00798
GN {ECO:0000313|EMBL:VCT89111.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF24451.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF24451.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF24451.1}, and DSM 44199 / CIP
RC 105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2] {ECO:0000313|EMBL:VCT89111.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT89111.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000268660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000268660};
RX PubMed=30701245; DOI=10.1128/mra.01522-18;
RA Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL Microbiol. Resour. Announc. 8:e01522-e01522(2019).
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; AMRA01000039; EKF24451.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT89111.1; -; Genomic_DNA.
DR RefSeq; WP_005626167.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BGZ9; -.
DR STRING; 1122247.GCA_000379865_01070; -.
DR KEGG; mhas:MHAS_00798; -.
DR PATRIC; fig|1122247.3.peg.1461; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 7328575at2; -.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR Proteomes; UP000268660; Chromosome 1.
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 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF44; BLR1022 PROTEIN; 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:VCT89111.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT DOMAIN 6..85
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..210
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 236..366
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 375 AA; 40256 MW; 113CAC7051146B06 CRC64;
MDFNLTNEQE LLRDGLTKFL ATRYDLEKSR AAAKTGAGWQ PDIWQGFAHE LGILGATLPE
EVGGIGGGPV ETMIIAEALG HALVVEPYID TVVVAGGLLL RAGGPVATAL LEQIVAGDAI
VTLAAAEEQS GDHWQQVATV AERDGDGWRL RGAKIVVPSA PLATHLLVTA RTDNGISLFV
VDVEAAGSGL EMHAYRTVDD HRAADIGFHD LRLPADALLG AEGQAWPSLE IARDEGAAAV
CAEAVGCMRK VLADTVEYTK QRQQFGQPIG SFQALQHRMV DMYMEVEQSV AAVYLATLNL
RSDPQTRARA VSAAKATIGR AARYVGQQAV QLHGGMGLTE ELAIGHYFKR LTALQYEFGS
TDYHVSRYTR LTRPS
//
