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Database: UniProt
Entry: A0A0M2HS44_9MICO
LinkDB: A0A0M2HS44_9MICO
Original site: A0A0M2HS44_9MICO 
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
//
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