ID Q740G6_MYCPA Unreviewed; 566 AA.
AC Q740G6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Glucose-methanol-choline oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=MAP_1385c {ECO:0000313|EMBL:AAS03702.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS03702.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS03702.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016958; AAS03702.1; -; Genomic_DNA.
DR AlphaFoldDB; Q740G6; -.
DR STRING; 262316.MAP_1385c; -.
DR KEGG; mpa:MAP_1385c; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_11; -.
DR Proteomes; UP000000580; 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 Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00411; PNDRDTASEI.
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 Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT DOMAIN 119..329
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 427..542
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 566 AA; 62050 MW; 45F43EAF7ED2AA27 CRC64;
MMGDFWRGLL KGAVGPRDND SRFLLDVHSR DLPGERTMRR YADDDEVDLV VVGAGAGGSV
LAQRLARAGW RVVVLEAGPF WHPDEDWVSD EAGSHPLYWT QKRIIGGADP IELGKNNSGR
GVGGSMIHYA GYTPRFHPSD FATYTLDRVG ADWPIRYEDL RRHYEQVELE LPVAGQNWPW
GDPHRYSFAP HPISGAAAKL WEGALKLGIE MRVGPVGIVN GTFGNRPHCI YRGYCLQGCK
VNAKASPYVT HLPDALAHDV EIRANCMAAR VELDGSGAAR GVVYYDEAGG TERLQRAKVV
AIAGYSIETP RLLLNSVSDR FPNGLGNNDD QVGRYVMVQG ATQSAGRWSE EVRMYKAPPP
EVTSEQFYET DSSRGFARGF SIQTVSPMPI GWAEHVLADG HWGRALREYM RDYNHWATIG
VLNELLPQPD NRVTLADEKD PYGIPVARFD YTLCDNDKAN MAYSTNVIGD ILRAADAQDV
LTIERFAHLI GGARMGTRPD NSVVDSDHRV WGVPNLLVAD GSVCPTQGSA NPALTIMALA
SRLAERLAAG KIDTAAGRRS KAAARG
//
