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Database: UniProt
Entry: A1U9K6_MYCSK
LinkDB: A1U9K6_MYCSK
Original site: A1U9K6_MYCSK 
ID   A1U9K6_MYCSK            Unreviewed;       514 AA.
AC   A1U9K6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ABL89514.1};
GN   OrderedLocusNames=Mkms_0297 {ECO:0000313|EMBL:ABL89514.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL89514.1};
RN   [1] {ECO:0000313|EMBL:ABL89514.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL89514.1};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000518; ABL89514.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1U9K6; -.
DR   STRING; 189918.Mkms_0297; -.
DR   KEGG; mkm:Mkms_0297; -.
DR   HOGENOM; CLU_011398_4_2_11; -.
DR   OrthoDB; 9813348at2; -.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..493
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   514 AA;  54279 MW;  FBFAC79AFA822FC3 CRC64;
     MSAFDEEVDV VVVGSGGGVA GAYTAAREGL SVALVEATER FGGTTAYSGG GGMWFPCNPV
     AQRAGIDDSP EDALAYFHRV VGDRTPLDLQ RAYVLGGPRL IEYLERDEHF QFAELPWPDY
     FGAVEHARAD GRRHIVPVPL PAADVGPQAA QIRGPLDAER LGHPVPALLT GGRALIGRFL
     AALARFPHAR THLGAPLVDL VDVDGAVVGA VINRDGENVR VRARRGVLLA AGGFEQNSRM
     RESFGVPGRA EDTMGCPGNT GAAHRAAIRV GAATDLMDQA WWSPGLTHPD GRSAFALWFT
     GGIFVDQRGE RFVNESAPYD RLGRAVIAEM DSRGMTLPFW MVYDDREGEV PPVKATNVSM
     VEAAQYRDAG LWRTADTLDT LADLIGVPAD ALTATVARFN AMVAGGRDTD FGRGDEPYDR
     AFSGGRSPMV AIEQPPFHAA AFGVSDLGTK GGLRTDTSAR VLDTDGRPIP GLYAAGNTMA
     AVSGTTYPGG GNPIGASLLF SHLAAMDMAG AGPR
//
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