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Database: UniProt
Entry: K6GJA7_9GAMM
LinkDB: K6GJA7_9GAMM
Original site: K6GJA7_9GAMM 
ID   K6GJA7_9GAMM            Unreviewed;       530 AA.
AC   K6GJA7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:EKO37091.1};
GN   ORFNames=B273_0080 {ECO:0000313|EMBL:EKO37091.1};
OS   SAR86 cluster bacterium SAR86E.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1208365 {ECO:0000313|EMBL:EKO37091.1, ECO:0000313|Proteomes:UP000010310};
RN   [1] {ECO:0000313|EMBL:EKO37091.1, ECO:0000313|Proteomes:UP000010310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAR86E {ECO:0000313|EMBL:EKO37091.1};
RA   Dupont C.L., Rusch D.B., Lombardo M.-J., Novotny M., Yee-Greenbaum J.,
RA   Laskin R.;
RL   Submitted (SEP-2012) 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, ECO:0000256|RuleBase:RU003968}.
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:EKO37091.1}.
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DR   EMBL; AMWX01000001; EKO37091.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6GJA7; -.
DR   STRING; 1208365.B273_0080; -.
DR   PATRIC; fig|1208365.4.peg.83; -.
DR   Proteomes; UP000010310; 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; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010310}.
FT   DOMAIN          82..105
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          254..268
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   530 AA;  58557 MW;  44A5A9CA3AE518F3 CRC64;
     MKFSHKYIIV GAGSAGCVLA NKLSEDPKNS VLLIEAGPMD NFSAIKMPLA ASSLFKNKKY
     GWCYETEPEI NLNNRAINWP RGKTLGGSSS INGMLYIRGQ AEDYENWESL GNPEWGYRDL
     IKYFINLENN QNYQDQFHGN FGPLWVETYE KNLDASLAFL EACKENNFKL NKDFNGSDQE
     GYGRYQVNIK NGKRFSSADA FLKPILDRPN LDLLTSTRVE KIIFSGKKAI GVKIKNAKGF
     NIIACTSEVI LSGGSINSPQ ILMLSGIGSK AQMERHGISC IKDIPGVGQN LQDHLTVNIS
     CKIKNLDTFS ELMTPFKMIN NLYEYYFSKN GLMTYPASDI GVFFKTNQNI SRPDAQIHFA
     PGAGKYNKNG AMKPSTGITA SVCNLRPKSR GHLELTSSRA DDSPKIVANY LSEPEDLKVM
     IDGVKRTREI FKTNVMKNLS ATETLPGKNC ITDQDIEEFI RNDALSVYHP VGTCKMGIGT
     ECVVNNDLTV KGLQGLRVAD ASIFPEIISG NTNATCNVIG AKCADLILKS
//
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