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Database: UniProt
Entry: Q1DC67_MYXXD
LinkDB: Q1DC67_MYXXD
Original site: Q1DC67_MYXXD 
ID   Q1DC67_MYXXD            Unreviewed;       781 AA.
AC   Q1DC67;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Oxidoreductase, GMC family {ECO:0000313|EMBL:ABF86668.1};
GN   OrderedLocusNames=MXAN_1504 {ECO:0000313|EMBL:ABF86668.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86668.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF86668.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR   EMBL; CP000113; ABF86668.1; -; Genomic_DNA.
DR   RefSeq; WP_011551615.1; NC_008095.1.
DR   AlphaFoldDB; Q1DC67; -.
DR   STRING; 246197.MXAN_1504; -.
DR   EnsemblBacteria; ABF86668; ABF86668; MXAN_1504.
DR   GeneID; 41358950; -.
DR   KEGG; mxa:MXAN_1504; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002483_1_0_7; -.
DR   OrthoDB; 337582at2; -.
DR   Proteomes; UP000002402; 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; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT   DOMAIN          90..292
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          487..550
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   781 AA;  84584 MW;  DF9C7F7D0901D660 CRC64;
     MRRLSSPWSE LASHYAVVVV GSGYGGAITA SRLARAGQQV CVLERGRELL PGDYPRTDAE
     FMSEFQVHFD PEAAADVGSP TALFELHRGG DVSVVTGCGL GGTSLINANV AMRPDPRVFL
     DGRWPDAFRA DVDGLLEDGF AWAEHMLRPL PYPESAPPLA TLSALAKSAE KLGGTFRRPP
     LAVTFEEGVN AAGVRQGACT LCGDCMTGCN FGAKNSVLMN YLPDAHRHGA KLFTEVGVRY
     LARDGARWRV YYRPMNAGRE RFDAPDLWLT ADRVILAAGT MGTAELLLRS KALGLSLSGR
     LGQRFSNNGD VMAFGYNTDV PVYGVGLGEA PSAGREPVGP TITGIIDDRA TLRQEDGMII
     ENGAIPAALA RPVTALLAAA SAIAGQDTDR GVIDRVGELA RIADSAVRGP YHGAMRNTQT
     FLVMSHDDGA GELRLSGDRV RVHWPGAGRQ AVFTRVDERL RRATEALGGT FVRNPLWNKL
     TGHELLCTHP LGGCAMGERA EEGVVDHEGR VFAGPEGTEV HEGLYVSDGS VIPRPLGINP
     LLTISAVAER TVALMARRHG WSVDYSPVPE APGPRPTQPL AVQFTETMYG YISAGADEDF
     LRAGDPARRD TSPFRFIVTV DSRDLEETLA HPLHPMQLSG CVVAPVLSSR PMTVERGVLH
     LMTHEGARPG GRRMRYQLPL VSESGERFFV DGYKDVHDDD GPDLWVDTTR LLVSIFRGED
     ASGRCIFRGY LRLNAKDFAV QLSTLRVLHA QGTVQRLAAL ARFGRFFFGE LFETYVRSKA
     A
//
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