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GLF_MYCGE
ID   GLF_MYCGE               Reviewed;         404 AA.
AC   Q49398;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=UDP-galactopyranose mutase;
DE            Short=UGM;
DE            EC=5.4.99.9;
DE   AltName: Full=UDP-GALP mutase;
DE   AltName: Full=Uridine 5-diphosphate galactopyranose mutase;
GN   Name=glf; OrderedLocusNames=MG137;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
CC   -!- FUNCTION: Involved in the conversion of UDP-GalP into UDP-GalF through
CC       a 2-keto intermediate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose;
CC         Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915;
CC         EC=5.4.99.9;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC       family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71354.1; -; Genomic_DNA.
DR   PIR; B64215; B64215.
DR   AlphaFoldDB; Q49398; -.
DR   SMR; Q49398; -.
DR   STRING; 243273.MG_137; -.
DR   EnsemblBacteria; AAC71354; AAC71354; MG_137.
DR   KEGG; mge:MG_137; -.
DR   eggNOG; COG0562; Bacteria.
DR   HOGENOM; CLU_042118_0_0_14; -.
DR   OMA; INVHKYG; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008767; F:UDP-galactopyranose mutase activity; IBA:GO_Central.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004379; UDP-GALP_mutase.
DR   InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR   Pfam; PF03275; GLF; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Isomerase; Reference proteome.
FT   CHAIN           1..404
FT                   /note="UDP-galactopyranose mutase"
FT                   /id="PRO_0000087509"
FT   BINDING         31
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..78
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         386..391
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  46661 MW;  67B8DAB814A3A680 CRC64;
     MNVILSVMLF SSPSCVNINS FDILIVGAGI SGIVLANILA NHNKRVLIVE KRDHIGGNCY
     DKVDSKTQLL FHQYGPHIFH TNNQTVINFI SPFFELNNYH HRVGLKLKNN LDLTLPFDFQ
     QIYKLMGKDG RKLVSFFKEN FSLNTHLSLA ELQLIDNPLA QKLYQFLISN VYKPYSVKMW
     GLPFAMINEN VINRVKIVLS EQSSYFPDAI IQGLPKSGYT NSFLKMLANP LIDVQLNCKD
     NLLVYQDEKL FFNNNLIEKP VVYCGLIDKL FNFCFGHLQY RSLAFSWKRF NQKKYQTYPV
     VNMPLAKSIT RSVEYKQLTN QGSFKPQTIV SFETPGSYAI NDPRFNEPYY PINNTLNDTL
     FKKYWKKASK LKNLHLLGRL ATYQYIDMDK AILLSIKKAQ QLLS
 
 
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