GAL7_NEUCR
ID GAL7_NEUCR Reviewed; 392 AA.
AC Q7RYE7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=gal-7; ORFNames=G21B4.010, NCU04460;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; BX908808; CAF05986.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA27793.1; -; Genomic_DNA.
DR RefSeq; XP_957029.1; XM_951936.2.
DR AlphaFoldDB; Q7RYE7; -.
DR SMR; Q7RYE7; -.
DR STRING; 5141.EFNCRP00000005235; -.
DR PRIDE; Q7RYE7; -.
DR EnsemblFungi; EAA27793; EAA27793; NCU04460.
DR GeneID; 3873213; -.
DR KEGG; ncr:NCU04460; -.
DR VEuPathDB; FungiDB:NCU04460; -.
DR HOGENOM; CLU_029960_0_0_1; -.
DR InParanoid; Q7RYE7; -.
DR OMA; HAIYYPP; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
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..392
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169890"
FT ACT_SITE 207
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 61
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 77..78
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 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 194
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 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 209
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 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 340
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 342
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 355..358
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 360..361
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 392 AA; 44890 MW; F7716BC5E28B4335 CRC64;
MTDKVLDDIS HRRYNPLNGS WLLVSPHRTK RPWQGQQEAP ALNKLPEYDP QCYLCPGNKR
AQGDSNPHYK NTFAFVNDYS AVKEEQQEYH PRKDAAGDGD DDIASLLLQA QPATGRCYVL
TFSAKHDTTL ADMSATEIVP VIETWTRIYA SHLSASHPLR DAAARSLSEI PPNPDGEVEP
AKKQQLRYMQ IFENKGAAMG CSNPHPHCQI WTTSTLPEEP GKELAQMTKY HREHKGRHLL
EDYVKVEMAK GERVVWQNDG FLVVCPWWAV WPFEVLVIAK RHVRALVELT SEERLQFAEA
VQEVTRRYDN LFETNFPYSS GIHQAPLDCT EEEAETSWFH MHFYPPLLRS ATVRKFLVGY
ELMAEPQRDI TPEQAAARLR DCGGELYRKS LQ
