ID I4EXQ4_9ACTN Unreviewed; 529 AA.
AC I4EXQ4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Pyranose oxidase {ECO:0000313|EMBL:CCH88167.1};
DE EC=1.1.3.10 {ECO:0000313|EMBL:CCH88167.1};
GN OrderedLocusNames=MODMU_2738 {ECO:0000313|EMBL:CCH88167.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88167.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88167.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88167.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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}.
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DR EMBL; FO203431; CCH88167.1; -; Genomic_DNA.
DR AlphaFoldDB; I4EXQ4; -.
DR STRING; 477641.MODMU_2738; -.
DR KEGG; mmar:MODMU_2738; -.
DR PATRIC; fig|477641.3.peg.2595; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_023699_0_0_11; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
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 SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:CCH88167.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 223..300
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 385..500
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 529 AA; 56239 MW; 1F30F5E8756BAD5C CRC64;
MRGSEMSRSF PPAVDVAIVG SGPNGAAYAR VLSERAPGAT IAVFEVGPAL TDPPGLHVKN
IADLDERLVA QRRSEGLRPH TATKEEAAYT DPTKRVVRAG THLLPDGFQQ PGEDGIPALA
MSSNVGGMGA HWTCACPRPG DAERPDFLPD LDELLDDAER LLGVSRDPFG SAPYSDVVRE
RLGAEFDPGR RAERRVRSMP LAVHVRDDGA LVWSGADVVF GEETRANPAA TLFPEAQVRR
VLVEDGRAVG VVVHDRRDGS DHEVRARFVV VAADALRTPQ LLFASGVRPP ALGRYLNDQP
QMVFAVRLRD VARTPEAEHD PRGDTAIVQQ SGVSWVPYTD EDPFHGQVMQ LDASPVPIVG
DDVPAPGTVV GLGWFCGKDL QASDRVEFDD TATDDYGMPK PRIHYTLTGQ DRETFARARD
SIRRAAAALG DPLGDEPFVL PSGASLHYQG TTRMGAVDDG TSVCGPTSEV WGVAGLYVAG
NNVIPTPMAC NPTLTSVALA IGGARDIADR LTADPSAVSA ESGGHAVPA
//