GAL7_SCHPO
ID GAL7_SCHPO Reviewed; 369 AA.
AC Q9HDU5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12 {ECO:0000250|UniProtKB:P09148};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=gal7; ORFNames=SPBPB2B2.10c;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-
CC glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989,
CC ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:66914; EC=2.7.7.12;
CC Evidence={ECO:0000250|UniProtKB:P09148};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09148};
CC Note=Binds 1 zinc ion per subunit. Zinc binding seems to play a
CC structural role. {ECO:0000250|UniProtKB:P09148};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07902}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAC21412.1; -; Genomic_DNA.
DR RefSeq; NP_596856.1; NM_001023879.2.
DR AlphaFoldDB; Q9HDU5; -.
DR SMR; Q9HDU5; -.
DR BioGRID; 277915; 1.
DR STRING; 4896.SPBPB2B2.10c.1; -.
DR MaxQB; Q9HDU5; -.
DR PaxDb; Q9HDU5; -.
DR PRIDE; Q9HDU5; -.
DR EnsemblFungi; SPBPB2B2.10c.1; SPBPB2B2.10c.1:pep; SPBPB2B2.10c.
DR GeneID; 2541407; -.
DR KEGG; spo:SPBPB2B2.10c; -.
DR PomBase; SPBPB2B2.10c; gal7.
DR VEuPathDB; FungiDB:SPBPB2B2.10c; -.
DR eggNOG; KOG2958; Eukaryota.
DR HOGENOM; CLU_029960_0_0_1; -.
DR InParanoid; Q9HDU5; -.
DR OMA; HAIYYPP; -.
DR PhylomeDB; Q9HDU5; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q9HDU5; -.
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:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; cd00608; GalT; 1.
DR Gene3D; 3.30.428.10; -; 2.
DR InterPro; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR019779; GalP_UDPtransf1_His-AS.
DR InterPro; IPR005850; GalP_Utransf_C.
DR InterPro; IPR005849; GalP_Utransf_N.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR11943; PTHR11943; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF000808; GalT; 1.
DR SUPFAM; SSF54197; SSF54197; 2.
DR TIGRFAMs; TIGR00209; galT_1; 1.
DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Galactose metabolism; Iron; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..369
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169891"
FT ACT_SITE 185
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 63
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 79..80
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 172
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 187
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 317
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 332..335
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 337..338
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
SQ SEQUENCE 369 AA; 42822 MW; B075514E2F9FDC63 CRC64;
MTSKKFDFTE YSHRRYNPLT DSYVLCSPHR AKRPWQGAKE EIKKDDTVKY DPTCYLCPGN
IRATGFENPK YETTYVFPND YPAVRVDQPD YMQDESEITK GNTLKTRMFK TEGVKGKCFV
ICFCPNHNLT LPLMSAEAIC NVVETWKHLY VTLKKESLEG PIRYKYLQIF ENKGSAMGCS
NPHPHGQAWC LDVIPSVVAQ EMCNMTKYFE LNNSHLLGDY VKLEMLEKER IVVENDSFIV
VVPYWALWPF ETLLIAKEHL KSLEEFEEKQ KVDLASALKM LTTKYDNLFN TSFPYSMGLH
QAPLYGSNEE VENSWFHMHF YPPLLRSATV KKFCVGFEML GEPQRDLTSE QAAARLQELD
GQKHYKNLL
