ID V9XMX2_9NOCA Unreviewed; 534 AA.
AC V9XMX2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:AHD23389.1};
GN ORFNames=Y013_23680 {ECO:0000313|EMBL:AHD23389.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD23389.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD23389.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD23389.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP006996; AHD23389.1; -; Genomic_DNA.
DR RefSeq; WP_024103558.1; NC_023150.1.
DR AlphaFoldDB; V9XMX2; -.
DR GeneID; 29938546; -.
DR KEGG; rpy:Y013_23680; -.
DR PATRIC; fig|1435356.3.peg.4773; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_2_11; -.
DR Proteomes; UP000018781; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 197..307
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 398..518
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 534 AA; 57534 MW; 1738E826179292DF CRC64;
MEQADVLIIG AGASGGVAAG ALAAAGFDVL CLEQGTWPDR TEYPAQRTTY ELEARKQWSG
SPNIRDKRVD YPINDAESAV APLMYAGVGG SMTLYAGDWP RLLPSDFRVR SLDGVADDWP
LRYADLQPFY ERTDSAFGVS GVGGDPAYPD GADPPLPPLP IGAIGRRMAR AHDALGWHWW
PAAQAVLSAP YGGRRPCVQF GACMQGCPEG AKASTDLTHW PTAVARGARL LTDARVSRVL
VSPQGLATGA EFVRSDGTWD VVHAEVVILA GNAIGTPRIL LNSASPEHPD GLANSSGLVG
RRLMVHPFAN VMGYFDDDMT SWQGHVGAKI ASYEFYETNP DRDFVRGAKW SLAPTGGPLN
AALPTRAGTD VWGEAHHDHV RRHLGRTISW GIFGEDLPDE ANTVEIDPDL TDSSGIPAPK
ITYRVSDNSR RLLDFHIARA TESLETAGAY DIATESLMRY SGWHLLGTAR MGNDPRTSVV
DQYGRCHDVP NLYIVDGSVF VTSGGVNPTS TIVALALRST EHLIAHRRHQ QVPA
//
