ID A0A0M9CD22_9ACTN Unreviewed; 555 AA.
AC A0A0M9CD22;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=FAD-binding dehydrogenase {ECO:0000313|EMBL:KOY49946.1};
GN ORFNames=ISGA_06675 {ECO:0000313|EMBL:KOY49946.1};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:KOY49946.1, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:KOY49946.1, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY49946.1,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:KOY49946.1}.
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DR EMBL; APHK02000029; KOY49946.1; -; Genomic_DNA.
DR RefSeq; WP_053776300.1; NZ_CP132196.1.
DR AlphaFoldDB; A0A0M9CD22; -.
DR STRING; 1241906.ISGA_06675; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008152; P: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; IPR014614; KsdD_DH.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR43260; 3-KETOSTEROID-DELTA-1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43260:SF1; KSDD-LIKE STEROID DEHYDROGENASE RV0785; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF036654; UCP036654; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989}.
FT DOMAIN 7..536
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 555 AA; 60302 MW; 8B719C31F0BA18A9 CRC64;
MTQQQADAIV VGAGLAGLVA TYELTQAGRK VIVVDQENRN NLGGQAFWSL GGLFLVDSPE
QRRLGIHDSA ELALQDWMGS AGFDREDEDY WPRQWARAYI DFAATEKRQY LHDLGLRITP
VVGWAERGGG FADGHGNSVP RFHLTWGTGP EVVRVFAEPV LEAERRGLVE FRFRHRVDEL
IVDDGAATGV RGALLEASDL DRGVASGREV VGEFEIRADA VIVTSGGIGH NHDLVRKNWP
TDRLGPAPEK MISGVPAYVD GRMLAITEDA GASLVNRDRM WNYTEGIVNW DPIWPDHAIR
IIPGPSSLWL DANGDRLPAP NFPGFDTNST MKAILATGHD YSWFILTQSI IEKEFALSGS
EQNPDITGKD LKFAAKSRLA KGAPGPVAAF VEHGEDFVVA DNLAELVTRM NGIARGPQLD
LRKIERVVSA RDAQVANKYS KDAQMMAITN ARQYLGDKVV RVAKPHRLLD PAHGPLIAVR
LNILTRKTLG GLETNLDSAV MRTDGTVFDG LYAAGEVAGF GGGGVHGYNA LEGTFLGGCI
FSGRAAGRAV ARRRP
//
