UAP1_SCHPO
ID UAP1_SCHPO Reviewed; 475 AA.
AC O94617;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
GN Name=uap1; Synonyms=qri1; ORFNames=SPBC1289.08;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB38688.1; -; Genomic_DNA.
DR PIR; T39359; T39359.
DR RefSeq; NP_596832.1; NM_001023853.2.
DR AlphaFoldDB; O94617; -.
DR SMR; O94617; -.
DR STRING; 4896.SPBC1289.08.1; -.
DR iPTMnet; O94617; -.
DR MaxQB; O94617; -.
DR PaxDb; O94617; -.
DR PRIDE; O94617; -.
DR EnsemblFungi; SPBC1289.08.1; SPBC1289.08.1:pep; SPBC1289.08.
DR GeneID; 2540183; -.
DR KEGG; spo:SPBC1289.08; -.
DR PomBase; SPBC1289.08; uap1.
DR VEuPathDB; FungiDB:SPBC1289.08; -.
DR eggNOG; KOG2388; Eukaryota.
DR HOGENOM; CLU_025603_1_1_1; -.
DR InParanoid; O94617; -.
DR OMA; KGMYRVG; -.
DR PhylomeDB; O94617; -.
DR Reactome; R-SPO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00533.
DR PRO; PR:O94617; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; ISO:PomBase.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISO:PomBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..475
FT /note="Probable UDP-N-acetylglucosamine pyrophosphorylase"
FT /id="PRO_0000185772"
FT MOTIF 103..106
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 301..302
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT BINDING 103..106
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 117
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 194
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 220
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 378
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 475 AA; 53121 MW; 3AF80295A682D7A3 CRC64;
MDDKELFDRS IFEETNQLHL YDQLNYLKKN DLQKFRKLLN QVQQLDLRSL WLKYRNAKAT
SQENRKLSPS EVGPLSIVDT SDSSWWRTGL REIARGHVAA LVLAGGQGTR LGFAGPKGCF
RLGLPNNPSI FELQAQKIKK SLALARAAFP DQEASISIPW YIMVSECTSE ETISFFKEND
FFGIDKKDVF FFQQGVLPCL DISGRVLFES DSSLAWAPNG NGGIYEALLS SGALNDMNRR
GILHITAYSV DNVLVLPVDP VFIGMATTKK LEVATKTVEK IDPAEKVGLL VSSHNHPCVV
EYSEISDEAC KATENVDGHK HLLLRAANIA YHYFSFDFLQ KASLHSSTLP IHLACKKIPF
YDVTSHHYTT PLNPNGYKLE SFIFDLFPSV SVENFGCFQV PRRTSFSPLK NSSKSPNDNH
ETCVNDILSL GKSWILKNGG ILSPSDCTYV SPECSLQGES LEWIKGKQVS NCKLY
