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YBB2_SCHPO
ID   YBB2_SCHPO              Reviewed;         414 AA.
AC   O60064;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Probable mannose-1-phosphate guanyltransferase;
DE            EC=2.7.7.13;
DE   AltName: Full=GDP-mannose pyrophosphorylase;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase;
GN   ORFNames=SPBC13G1.02;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC       glycosylation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC         alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58409; EC=2.7.7.13;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA18655.1; -; Genomic_DNA.
DR   PIR; T39403; T39403.
DR   RefSeq; NP_596551.1; NM_001022472.2.
DR   AlphaFoldDB; O60064; -.
DR   SMR; O60064; -.
DR   BioGRID; 276303; 4.
DR   STRING; 4896.SPBC13G1.02.1; -.
DR   iPTMnet; O60064; -.
DR   MaxQB; O60064; -.
DR   PaxDb; O60064; -.
DR   PRIDE; O60064; -.
DR   EnsemblFungi; SPBC13G1.02.1; SPBC13G1.02.1:pep; SPBC13G1.02.
DR   GeneID; 2539751; -.
DR   KEGG; spo:SPBC13G1.02; -.
DR   PomBase; SPBC13G1.02; -.
DR   VEuPathDB; FungiDB:SPBC13G1.02; -.
DR   eggNOG; KOG1460; Eukaryota.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; O60064; -.
DR   OMA; MPVPNWW; -.
DR   PhylomeDB; O60064; -.
DR   UniPathway; UPA00126; UER00930.
DR   PRO; PR:O60064; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; ISS:PomBase.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IC:PomBase.
DR   GO; GO:0006486; P:protein glycosylation; IC:PomBase.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..414
FT                   /note="Probable mannose-1-phosphate guanyltransferase"
FT                   /id="PRO_0000311772"
SQ   SEQUENCE   414 AA;  46096 MW;  D0182B33936935A2 CRC64;
     MISSAVILVG GPSRGTRFRP LSFDVPKPLF KIGGREMIYH HLAALSKIES VKDVFLVGFY
     DESVFKDFIN EVASHFPSFN RIKYLREYNC LGTGGGLYHF RDQILKGHTS NVFVMHADVC
     CSFPLQELLN VHHEKKALVT LMATKVSKED ASNFGCLVEE PSTGRVLHYV DKPSSYLSNI
     ISCGIYIFDA SIFDEIKKAY ERRLEEVEKQ LRSLDEGMED YLSLETDVLA PLCSDSSKAI
     YAYNTPEFWR QIKTAGSAVP ANSLYLQKAY HDGTLPKPDT EAEIIQPVFI HPNAIVSKGA
     KIGPNVSIGA RVRIEDGARI RNSIIQEDCE ISANAVVLHS ILSRHCKIGK WSRVEGSPTL
     PSQHSTTIMR NSVKVQAITV MGADCIVHDE VRVQNCLVLP HKEIKVGLVG EIVM
 
 
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