ID A0A0G3IMM1_9MYCO Unreviewed; 487 AA.
AC A0A0G3IMM1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN ORFNames=AB431_17075 {ECO:0000313|EMBL:AKK28109.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK28109.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK28109.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK28109.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP011773; AKK28109.1; -; Genomic_DNA.
DR RefSeq; WP_047330931.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IMM1; -.
DR STRING; 1545728.AB431_17075; -.
DR KEGG; mye:AB431_17075; -.
DR PATRIC; fig|1545728.4.peg.3481; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000035237; Chromosome.
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; 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 23..452
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 487 AA; 51618 MW; AF2EB3617F587C49 CRC64;
MSGLDIPTTV AASDVTEWSD EFDVVVIGFG IGGGCAAVSA AAAGARVLVL ERAAVAGGTT
SMAGGHFYLG GGTAVQKATG HSDSVEEMYK YLVAVSREPE LDKIRAYCEG SVEHFDWLEE
LGIAFERSYY PEKAVIQPNT EGLMFTGNEK VWPYKNMAVP APRGHKVPVP GDTQGAAMVI
DLLLKRCAEL GVQIRYETGA TNLVVDGDSV VGVSWKKFTE TGSIRAKAVV IAAGGFVMNP
EMVAKLTPKL AEKPFVLGNT YDDGLGIRLG ESVGGATKHM DQIFITAPVY PPSILLTGII
VNKEGKRFVT EDSYHSRTSG FVMDQPDSAA YLIVDEAHMQ RPEIPLITFI DGWETVEEME
AALGIPPGNL VETLNNYNKY AAQGEDPEFH KQPEFLAPQD KGPWGAFDLT LGKAMYSGFT
VGGLATDVDG EVLRDDGSVI PGLYAAGACA SNIAQDGKGY ASGTQLGEGS FFGRRAGTHA
AKVALGG
//
