GenomeNet

Database: UniProt
Entry: A1UG86_MYCSK
LinkDB: A1UG86_MYCSK
Original site: A1UG86_MYCSK 
ID   A1UG86_MYCSK            Unreviewed;       392 AA.
AC   A1UG86;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Acyl-CoA dehydrogenase, type 2, C-terminal domain {ECO:0000313|EMBL:ABL91844.1};
GN   OrderedLocusNames=Mkms_2649 {ECO:0000313|EMBL:ABL91844.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL91844.1};
RN   [1] {ECO:0000313|EMBL:ABL91844.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL91844.1};
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL91844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UG86; -.
DR   STRING; 189918.Mkms_2649; -.
DR   KEGG; mkm:Mkms_2649; -.
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   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; 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; PF08028; Acyl-CoA_dh_2; 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          240..368
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   392 AA;  42767 MW;  BA5E5BC734DEE3E1 CRC64;
     MTVTTQRTST LADRVRDILP GISARADEAE RIRKVPVQNV DALREIGFFR AFVPAKYDGL
     SVLPSEFGEA TRVLATACPS TAWACGLMAV HAHTVANYSP VLQEEVWGSD PDTLICSSVA
     PMGQPTKVDG GIRLTGDFSW SSGSEHAHWI IVGMMMPGSS EAPEPHFAIV PRSDFEIKDT
     WFAMGLKGTG SQDISIKDVF VPEYRLETLI SLNIGTATGF GTHDAPVYRL PWQPVFALNF
     SAVNLGASEA LRDLYPARLS TRVRAYTGAK VGETAPALMR LAESTHELDA ARSLLESDWR
     AMDSRANSTD PTTPDEMAGW RSNQAYITRL AVRAADRLFD ASGGSAVRDE NPMQRYWRDL
     HTGAAHTYSD YDIAAQVYGA HLAAVQPQEG LF
//
DBGET integrated database retrieval system