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GAL10_KLULA
ID   GAL10_KLULA             Reviewed;         688 AA.
AC   P09609; Q6CKS7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 147.
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; OrderedLocusNames=KLLA0F08415g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=3419917; DOI=10.1093/nar/16.16.8192;
RA   Webster T.D., Dickson R.C.;
RT   "Nucleotide sequence of the galactose gene cluster of Kluyveromyces
RT   lactis.";
RL   Nucleic Acids Res. 16:8192-8194(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- INDUCTION: By galactose.
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; X07039; CAA30090.1; -; Genomic_DNA.
DR   EMBL; CR382126; CAG98170.1; -; Genomic_DNA.
DR   PIR; S01407; XUVKG.
DR   RefSeq; XP_455462.1; XM_455462.1.
DR   AlphaFoldDB; P09609; -.
DR   SMR; P09609; -.
DR   STRING; 28985.XP_455462.1; -.
DR   EnsemblFungi; CAG98170; CAG98170; KLLA0_F08415g.
DR   GeneID; 2894953; -.
DR   KEGG; kla:KLLA0_F08415g; -.
DR   eggNOG; KOG1371; Eukaryota.
DR   HOGENOM; CLU_007383_22_0_1; -.
DR   InParanoid; P09609; -.
DR   OMA; KGLYREW; -.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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; IEA:UniProtKB-EC.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:EnsemblFungi.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW   Multifunctional enzyme; NAD; Reference proteome.
FT   CHAIN           1..688
FT                   /note="Bifunctional protein GAL10"
FT                   /id="PRO_0000197439"
FT   REGION          1..346
FT                   /note="Galactowaldenase"
FT   REGION          347..688
FT                   /note="Mutarotase"
FT   ACT_SITE        525
FT                   /note="For mutarotase activity"
FT                   /evidence="ECO:0000255"
FT   BINDING         6..37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        199..201
FT                   /note="DPL -> AF (in Ref. 1; CAA30090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   688 AA;  76359 MW;  1BB0087A2D6C574A CRC64;
     MSEDKYCLVT GGAGYIGSHT VVELCEAGYK CIVVDNLSNS SYESVARMEL LTGQEIKFAK
     IDLCELEPLN KLFDDYKIDS VLHFAGLKAV GESTQIPLTY YFNNIVGTIN LLECMKSHDV
     KKLVFSSSAT VYGDATRFEN MIPIPETCPT GPTNPYGKTK LTIEDMMRDL HFSDKSFSFA
     ILRYFNPIGA HPSGVIGEDP LGIPNNLLPF MAQVAIGRRP KLYVFGDDYD SVDGTPIRDY
     IHVVDLAKGH LAALKYLEKY AGTCREWNLG TGHGTTVLQM YRAFCDAIGF NFEYVVTARR
     DGDVLNLTAK CDRATNELEW KTELDVNKAC VDLWKWTQDN PFGYQIKGVD SKFFGDKGDF
     SSRVVSLGKG TSFEVKLANL GATIVDIVVN GCSVVASLDN ETEYKDQSNP FFGATVGPYA
     NRIANGTFEI NGKRIQLTVS KEDGNVVHSG INSYHSKKFL GPIVKNPEAH IWTADFKYVD
     EETEFPARLS TLVRYKVDSE KKTLTVEYES KVAGQGSTGA NITNHTYFNL NKFNEATIKG
     SKVQLIDNTG LEVNNKLLPT GNLKKYTQVA TFNDSPTEIT EKEPVLDFCF VSGLPAKLDT
     RSSPLTPVFK LSNEDAKLEV EVATTEPTFQ VYTGDYVDVK DKYENRAGIC CEPGRYIDAV
     NNPEWKSSVV LPAGETYGHK LSYTFRTL
 
 
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