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Database: UniProt
Entry: A0A075P0Q1_9ALTE
LinkDB: A0A075P0Q1_9ALTE
Original site: A0A075P0Q1_9ALTE 
ID   A0A075P0Q1_9ALTE        Unreviewed;       541 AA.
AC   A0A075P0Q1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:AIF99363.1};
GN   ORFNames=EP13_12085 {ECO:0000313|EMBL:AIF99363.1};
OS   Alteromonas australica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF99363.1, ECO:0000313|Proteomes:UP000056090};
RN   [1] {ECO:0000313|EMBL:AIF99363.1, ECO:0000313|Proteomes:UP000056090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 17 {ECO:0000313|EMBL:AIF99363.1,
RC   ECO:0000313|Proteomes:UP000056090};
RA   Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT   "Genomes of Alteromonas australica, a world apart.";
RL   Submitted (JUN-2014) 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}.
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DR   EMBL; CP008849; AIF99363.1; -; Genomic_DNA.
DR   RefSeq; WP_044057460.1; NZ_CP008849.1.
DR   AlphaFoldDB; A0A075P0Q1; -.
DR   GeneID; 78255642; -.
DR   KEGG; aal:EP13_12085; -.
DR   eggNOG; COG2303; Bacteria.
DR   Proteomes; UP000056090; 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; 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.
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:UP000056090}.
FT   DOMAIN          85..108
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          257..271
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   541 AA;  59291 MW;  2D0318CD56C00D4A CRC64;
     MSDSNTQFDY IIVGAGSAGG VMAARLSEDP ALRVLLIEAG SKDSNPFIHI PFGLSILSRF
     EGIGWGYHTT VQGELHDREL FWPRGKTLGG SSSVNAMCYI RGQKEDYDRW AQEGAEGWGF
     DEVLPYFKRS ENYYQGEDDY HGVGGPLHVS PLTDTSRLSD AFLAAAPAAD LAVLDDFNRD
     VREGLGYYHV TQVNGQRCST AKGYLSQAKH RGNLVILTKV AVEKVLIKNK CAIGVQAREK
     GNVKRYAARQ EVILCGGAIN SPHLLMLSGV GPRRQLENMG IYVHLDLPGV GENLQDHLDA
     IVQNTCKAKE GYAVAAGMFP KYAKASVEYL FKRKGIFSSN IAEAGGFVRS SIADDYPDIQ
     FHFLPAILED HGRQLAFGYG YGVHVCCLYP KSRGTIRLQS NHPADHPLID PKYLTHPDDI
     KVMIDGIKLA RTLLAAPSFA PFEGKERHPG EDAQTDEDLT AFLRERAETI YHPIGTCKMG
     KESDPMAVVN NKLKVLGIEN LRVVDASVMP SLVGGNTNAP TIMIAERAVD FIKAELHQAA
     L
//
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