ID A0A0M2HS44_9MICO Unreviewed; 484 AA.
AC A0A0M2HS44;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alcohol dehydrogenase [acceptor] {ECO:0000313|EMBL:KJL47730.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:KJL47730.1};
GN Name=alkJ {ECO:0000313|EMBL:KJL47730.1};
GN ORFNames=RS84_02529 {ECO:0000313|EMBL:KJL47730.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL47730.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL47730.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL47730.1,
RC ECO:0000313|Proteomes:UP000033900};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:KJL47730.1}.
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DR EMBL; JYJB01000009; KJL47730.1; -; Genomic_DNA.
DR RefSeq; WP_045258070.1; NZ_JYJB01000009.1.
DR AlphaFoldDB; A0A0M2HS44; -.
DR STRING; 273678.RS84_02529; -.
DR PATRIC; fig|273678.4.peg.2534; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000033900; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:KJL47730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033900}.
FT DOMAIN 231..245
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 11..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 484 AA; 51659 MW; 55EC53B1ACF64557 CRC64;
MRSAIVVGAG TSGAIVARRL VDAGVDVTLV EAGGYDTNPA IHDPSRAGEL WHSAEDWDYF
TVPQQHAAGR RLHLPRGRVT GGSHALNAMI WVRGAASDYD GWERDGATGW AWSDVEPVYE
AIENDLLPVT GDYPLSPIQA SIIDAAVQEG LPHNANYNGG TLDGVSQEQV TMRDGRRVNT
WMAYAQPVAD RLTVVTGREV HSVIIEDGRA LGVRFEDGEE LRADEIVLSA GALGSPVILM
RSGIGPAAEL EALGISVVRD SPQVGKNLHD HLLSPVIFTT SREVGPPQPG VSVTQTHLFW
RSRPELAEPD TQPIHFSVPM WGELEPRGDD GFTLMAGLIT PHSRGSLTLS GPAVSDPPLI
DLAALTDERD VASLAASVRQ CRRIGAQPAL AGEWGAVEVY PGPEVAEGDV EDWVRRTAIT
YHHQVGTCRM GSDADAVVDP GLRVRGIDGL RVIDASVMPT VPSGNTNAPA AMIAERGARF
LLEG
//