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Database: UniProt
Entry: B2HHC1_MYCMM
LinkDB: B2HHC1_MYCMM
Original site: B2HHC1_MYCMM 
ID   B2HHC1_MYCMM            Unreviewed;       657 AA.
AC   B2HHC1;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Oxidoreductase GMC-type {ECO:0000313|EMBL:ACC40053.1};
GN   OrderedLocusNames=MMAR_1602 {ECO:0000313|EMBL:ACC40053.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40053.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40053.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP000854; ACC40053.1; -; Genomic_DNA.
DR   RefSeq; WP_012393436.1; NC_010612.1.
DR   AlphaFoldDB; B2HHC1; -.
DR   STRING; 216594.MMAR_1602; -.
DR   KEGG; mmi:MMAR_1602; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_008878_3_0_11; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000001190; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          395..409
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   657 AA;  69025 MW;  5A118391134B66A6 CRC64;
     MNSPVTDTHR AVLAALADTV VPSLDRSDDP TRFWSLGGSD LHADVAVGFT LAELPEQQRA
     GMLALLDGLH AQGFVAASQS ARERLIGDFA QLGPQPAAAM NALVSLTLAV AYAGPDPQTA
     SNPMWEGFGY PGAPRIEPGG DEAPVPFVPD GPELSADVCV VGSGAGGGLI AGVLAQAGLD
     VVVLEAGGNF NEPDFSGLEL PAFQQMFWRG GPTPTADFNV TLLAGATLGG GPTINWSNCL
     RTPAQVREQW AQEFGLKDVD GPEFDRHLDA VWERLGVNPD CSDLNGPHER MRDGAQELGW
     SFKTLFRNAD PAAYSPDTAG YIGLGDRSGA KLDVRRTYLR DAVHSGARVI ARCRAERVLT
     RDGRATGVQA SFVDPRTGAS VPLQVNAPRV VAACGSLESP ALLLRSGIGG PAVGRYLHLH
     PVVAMLALHD QPQQPWWGGP MTALVDEFSD IEDGYGFLIE GAQWATSIIA GGMARATFEE
     HKETMARLGN AAWLIGLARD RGHGTVTIDD AGEAVVHYDL TDELDVRIAH QSIEAQIRIH
     AAGGAREIVP FAATGARWRA GDDLEAFIAE MQRIPLGAGG HRLFSAHQMS SCRMGSDPAT
     SVANEWGELH DTPGVFIGDA SALPSASGAN PMISTMALAH RTAEAIAAIA VPGGGNA
//
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