ID B2HG67_MYCMM Unreviewed; 584 AA.
AC B2HG67;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ACC43179.1};
GN OrderedLocusNames=MMAR_4775 {ECO:0000313|EMBL:ACC43179.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43179.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC43179.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000854; ACC43179.1; -; Genomic_DNA.
DR AlphaFoldDB; B2HG67; -.
DR STRING; 216594.MMAR_4775; -.
DR KEGG; mmi:MMAR_4775; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_2_11; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000001190; Chromosome.
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; 2.
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 PRINTS; PR00411; PNDRDTASEI.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 14..551
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 584 AA; 62624 MW; 04B18A4DF9708D84 CRC64;
MTVGPWGDVD RMVDVLVVGS GGGGMTAALT AASSGLDTLV IEKSSCFGGS TALSGGGIWV
PGAPAQRRAG YSPNPDDVVG YLRRITDGLV SEARIRQYVY SAPQMLEFLE GLSAWLEFVW
KPGYADYYPE LPGGSVLGST INVPPIDLRK LGDDQPRLLT PLALAPRGIW LGPKELRSFY
RIRQSWAGKA VLLKLVTRMI RARVFGEQIA AIGQSLAARL RLAMKELGVA LWLDAPLVEL
LTDAGGAVTG AVVQTEGGRE RIGVRGGVIL ASGGFDHDLA WRKEHQPLVE QDWSFGNPAA
LGDGIRAGQR VGAAADLLDE AWWFPAIQWP DGRMQFMLNE RMMPAQFIVN GAGKRFINEA
APYMDFGHAM IAGQKSGVTH IPCWLVTDHR SFNRYVVAGH LPIPKIPGAP VPTGRKIPTA
WLESGVVKAA TSWAELATKV GVPGGQLQAT AERFNELAVK GHDEDFNRGD SVYDNYYGDP
TLPNPNLYPL GDPPYYAFRI VLGDLGTSGG LRTDEYARVL RPDDTTVGGL YAVGNTSAPV
MGRSYAGAGA TIGPAMTFGF VAAKHLAAQL DARRATPTTH LHGR
//
