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Database: UniProt
Entry: A0A1B9D3C7_MYCMA
LinkDB: A0A1B9D3C7_MYCMA
Original site: A0A1B9D3C7_MYCMA 
ID   A0A1B9D3C7_MYCMA        Unreviewed;       560 AA.
AC   A0A1B9D3C7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=3-ketosteroid-delta-1-dehydrogenase {ECO:0000313|EMBL:OCB49652.1};
GN   ORFNames=A5677_24495 {ECO:0000313|EMBL:OCB49652.1};
OS   Mycobacterium malmoense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB49652.1, ECO:0000313|Proteomes:UP000092683};
RN   [1] {ECO:0000313|EMBL:OCB49652.1, ECO:0000313|Proteomes:UP000092683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3012 {ECO:0000313|EMBL:OCB49652.1,
RC   ECO:0000313|Proteomes:UP000092683};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OCB49652.1}.
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DR   EMBL; MBEE01000176; OCB49652.1; -; Genomic_DNA.
DR   RefSeq; WP_065472360.1; NZ_MBEE01000176.1.
DR   AlphaFoldDB; A0A1B9D3C7; -.
DR   OrthoDB; 9813348at2; -.
DR   Proteomes; UP000092683; Unassembled WGS sequence.
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   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}.
FT   DOMAIN          7..541
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   560 AA;  60442 MW;  3391F6BE0EEF1F42 CRC64;
     MTAQELDVVV VGSGGAGMVA ALTAAHRGLS TVVIEKAAHY GGSTARSGGG VWIPNNEILK
     RDGVRDNPEA ARTYLHGIVG NVVEPERIDT YLDRGPEMLS FVLEHTPLKM CWVPRYSDYY
     PEAPGGRAEG RSIEPKPFDA RKLGADMPGL EPAYGKVPLN VVVMQQDYVR LNQLKRHPRG
     VLRSLKVGAR TMWAKATGKN LVGMGRALIG PLRIGLQRAG VPVLLNTALT DLYVEDGVVR
     GVYVRDTGAS ESSEPRLIRA RRGVILASGG FEHNEQMRVK YQRAPITTEW TVGAKANTGD
     GIVAAEKLGA ALELMEDAWW GPTVPLVGAP WFALSERNSP GSIIVNMSGK RFMNESMPYV
     EACHHMYGGE FGQGPGPGEN IPAWLVFDQQ YRDRYIFAGL QPGQRIPRKW LESGVIISAD
     TLEELAQKAG LPVADFAATV ARFNGFARSG VDEDFHRGES AYDRYYGDPT NKPNPNLGEL
     THAPYYAAKM VPGDLGTKGG VRTDVHGRAL RDDGTIIEGL YAAGNVSAPV MGHTYPGPGG
     TIGPAMTFGY LAALHIAGER
//
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