ID A4T5J8_MYCGI Unreviewed; 394 AA.
AC A4T5J8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Acyl-CoA dehydrogenase, type 2, C-terminal domain {ECO:0000313|EMBL:ABP43945.1};
GN OrderedLocusNames=Mflv_1463 {ECO:0000313|EMBL:ABP43945.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43945.1};
RN [1] {ECO:0000313|EMBL:ABP43945.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43945.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP43945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43945.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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DR EMBL; CP000656; ABP43945.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T5J8; -.
DR STRING; 350054.Mflv_1463; -.
DR KEGG; mgi:Mflv_1463; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_11; -.
DR OrthoDB; 3404950at2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd01159; NcnH; 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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PTHR48083:SF19; FLAVIN-DEPENDENT MONOOXYGENASE, OXYGENASE SUBUNIT HSAA; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
FT DOMAIN 22..99
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 240..372
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 394 AA; 43200 MW; F70F4B7BCB26B312 CRC64;
MTSIEQRDAQ TVLAGVNDLL PRIAKRSAAA EELRRLPDET VAELDEVGFF KLLQPEQWGG
LQCDPTLFYE AVRRIASACG STGWVSSIIG VHNWHLALFD QKAQEDVWGD DPTVRVSSSY
APMGAGTVVD GGYLVSGAWQ WSSGCDHATW AFLGGPVIKD GKPVDFGSFL IPRTDYRIDD
VWNVVGLKAT GSNTVVVKDV FVPRHRFLSY KAMNDGTAGG YENNTAPVYK MPWGTMHPTT
ISAPIMGMAY GAYEAHVEHQ GKRVRAAFAG EKSKDDPFAK IRIAEAASDI DAGWRQLIGN
VRDEYELLQA GKEIPFSLRA SARRDQVRAT ARAIASIDLL FEASGATALQ LDQPVQRFWR
DAHAGRVHAA NEPERAYLIF GNDAFGLPPQ DTMV
//
