ID   A0A136HTG6_9ALTE        Unreviewed;       559 AA.
AC   A0A136HTG6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:KXJ58923.1};
GN   ORFNames=AXW14_01400 {ECO:0000313|EMBL:KXJ58923.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ58923.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KXJ58923.1}.
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DR   EMBL; LSMP01000232; KXJ58923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136HTG6; -.
DR   Proteomes; UP000070342; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 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          61..322
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          420..545
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   559 AA;  61134 MW;  98882E44FD87FFD2 CRC64;
     MDDFDYHAVV VGSGAGGAMA AYELTRQGIK VLLLEAGRDY DPKAETPMFK TNHEAPLLGS
     SNKDKNFGFY DATVDGGWQV PDEPYTTAEG SEFMWWRARM LGGRTNHWGR YSLRFSHHDF
     KGKSRDGLGA DWPFEYDDIA PWYDKTEKLV GVCGANTDHE DMPHSAPGVL QEPPKPRVTE
     LLVAAAAGKE GIRAVPMHRA VLTKSQDIRQ KCFYATPCGH GCSIGAAFQT TTSLIPLAKQ
     TGNLKVITDA MVRTVDTDSD GQVTGLTYVD KNTGKDIKLL SKVVILAASS CESARILLNS
     KTDVHPAGLA NSSGQVGRNL MDSTGAGIGA YIPALRNRPR YNEDGHTANH LFIPWWGHDA
     QAKGELDFPR GYHFEIGSGF REPGSWVAGD FQGYGLSVKE EARAAYGSYI SFALRGEMLP
     NDNCYMEIDD EVTDKWGIPV AKFHWKFSEH EINQVKHGLE TAKKIFANMG ADVGDLPAPE
     DAILKGGQII HEVGATRMGE DPADSVTNQW GQTWDCPNLF VMDAGTFASN PHKNCTLTIL
     TLAMRNADWL AGQIKQGAL
//