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GAL10_SCHPO
ID   GAL10_SCHPO             Reviewed;         713 AA.
AC   Q9HDU3;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Bifunctional protein gal10;
DE   Includes:
DE     RecName: Full=UDP-glucose 4-epimerase;
DE              EC=5.1.3.2;
DE     AltName: Full=Galactowaldenase;
DE   Includes:
DE     RecName: Full=Aldose 1-epimerase;
DE              EC=5.1.3.3;
DE     AltName: Full=Galactose mutarotase;
GN   Name=gal10; ORFNames=SPBPB2B2.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC       active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC       lactose (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC         Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC         EC=5.1.3.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC         ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10126};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC       epimerase/dehydratase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC       family. {ECO:0000305}.
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DR   EMBL; CU329671; CAC21414.1; -; Genomic_DNA.
DR   RefSeq; NP_596858.1; NM_001023881.2.
DR   AlphaFoldDB; Q9HDU3; -.
DR   SMR; Q9HDU3; -.
DR   BioGRID; 277919; 6.
DR   STRING; 4896.SPBPB2B2.12c.1; -.
DR   iPTMnet; Q9HDU3; -.
DR   MaxQB; Q9HDU3; -.
DR   PaxDb; Q9HDU3; -.
DR   EnsemblFungi; SPBPB2B2.12c.1; SPBPB2B2.12c.1:pep; SPBPB2B2.12c.
DR   GeneID; 2541411; -.
DR   KEGG; spo:SPBPB2B2.12c; -.
DR   PomBase; SPBPB2B2.12c; gal10.
DR   VEuPathDB; FungiDB:SPBPB2B2.12c; -.
DR   eggNOG; KOG1371; Eukaryota.
DR   HOGENOM; CLU_007383_22_1_1; -.
DR   InParanoid; Q9HDU3; -.
DR   OMA; KGLYREW; -.
DR   PhylomeDB; Q9HDU3; -.
DR   BRENDA; 5.1.3.2; 5613.
DR   Reactome; R-SPO-70370; Galactose catabolism.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:Q9HDU3; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IMP:PomBase.
DR   GO; GO:0006012; P:galactose metabolic process; IMP:PomBase.
DR   GO; GO:0042125; P:protein galactosylation; IMP:PomBase.
DR   GO; GO:0052574; P:UDP-galactose biosynthetic process; IMP:PomBase.
DR   CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005886; UDP_G4E.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR01179; galE; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW   Multifunctional enzyme; NAD; Reference proteome.
FT   CHAIN           1..713
FT                   /note="Bifunctional protein gal10"
FT                   /id="PRO_0000197441"
FT   REGION          1..350
FT                   /note="Galactowaldenase"
FT   REGION          351..713
FT                   /note="Mutarotase"
FT   ACT_SITE        532
FT                   /note="For mutarotase activity"
FT                   /evidence="ECO:0000255"
FT   BINDING         7..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   713 AA;  80666 MW;  51C89DA0843A8556 CRC64;
     MAVQDEYILV TGGAGYIGSH TVIELINHGY KVIIVDNLCN SCYDAVARVE FIVRKSIKFF
     KLDLRDKEGL AQIFDTFKIK GVIHFAALKA VGESMKLPLE YYDNNICGTI TLLNVMREHR
     VKTVVFSSSA TVYGDATRFD NMIPIPESCP NDPTNPYGKT KYAIENIIKD LHTSDNTWRG
     AILRYFNPIG AHPSGLLGED PLGIPNNLLP FLAQVAIGRR EKLLVFGDDY DSHDGTPIRD
     YIHVVDLAKG HIAALNYLNK INNSEGMYRE WNLGTGKGSS VFDIYHAFCK EVGKDLPYEV
     VGRRTGDVLN LTASPNRANS ELKWKAELSI TDACRDLWKW TIENPFGFQI DNYKWKLFNT
     LGIMDYKNRL HTICFQDLEV SIANYGALVQ AVRYKGRNLV NGFNDFSRYK LKENPFFGAT
     IGRFANRIAN GQFEVDGHLY TLCKNENNKT TLHGGNNGFD KQFFLGPIAR QYEDYNTLEF
     ILVDKDGNNG FPSDLETLVK YTIKNNSLEI EYKSVIPEYS KLNVTAVNLT NHSYWNLASP
     NKTIDGTIIK STTNVYLKVN SETSLPTGDI VEWQNDITKP TKLDPNISFD NCFIVDREAS
     KFCLDTRKYS LKNIVEVIHP SVPVKLVVST TEPAFQLYTG DGNDICEFQS RSGFCVETGR
     FINALNNEKW SKQVILRKGE VYGARSKFSL YAQDLEENKH FLDSASYNSG EYY
 
 
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