GALT_MOUSE
ID GALT_MOUSE Reviewed; 379 AA.
AC Q03249; Q91VQ7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12 {ECO:0000250|UniProtKB:P07902};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=Galt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1427861; DOI=10.1016/s0888-7543(05)80244-7;
RA Leslie N.D., Immerman E.B., Flach J.E., Florez M., Fridovich-Keil J.L.,
RA Elsas L.J.;
RT "The human galactose-1-phosphate uridyltransferase gene.";
RL Genomics 14:474-480(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C129;
RA Velicescu M., Reichardt J.K.V., Dubeau L.;
RT "Mouse galactose-1-phosphate uridyl transferase (GalT) gene.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays an important role in galactose metabolism.
CC {ECO:0000250|UniProtKB:P07902}.
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:P07902};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07902};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:P07902};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000250|UniProtKB:P07902}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07902}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37658.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA83562.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10985.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M96265; AAA37658.1; ALT_FRAME; mRNA.
DR EMBL; U41282; AAA83562.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC010985; AAH10985.2; ALT_INIT; mRNA.
DR RefSeq; NP_057867.2; NM_016658.3.
DR AlphaFoldDB; Q03249; -.
DR SMR; Q03249; -.
DR STRING; 10090.ENSMUSP00000081745; -.
DR iPTMnet; Q03249; -.
DR PhosphoSitePlus; Q03249; -.
DR EPD; Q03249; -.
DR jPOST; Q03249; -.
DR MaxQB; Q03249; -.
DR PaxDb; Q03249; -.
DR PRIDE; Q03249; -.
DR ProteomicsDB; 268844; -.
DR DNASU; 14430; -.
DR GeneID; 14430; -.
DR KEGG; mmu:14430; -.
DR UCSC; uc008sjo.2; mouse.
DR CTD; 2592; -.
DR MGI; MGI:95638; Galt.
DR eggNOG; KOG2958; Eukaryota.
DR InParanoid; Q03249; -.
DR OrthoDB; 1135699at2759; -.
DR PhylomeDB; Q03249; -.
DR BRENDA; 2.7.7.12; 3474.
DR Reactome; R-MMU-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR BioGRID-ORCS; 14430; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Galt; mouse.
DR PRO; PR:Q03249; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q03249; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:MGI.
DR GO; GO:0006012; P:galactose metabolic process; IMP:MGI.
DR GO; GO:0061623; P:glycolytic process from galactose; IMP:MGI.
DR GO; GO:0006258; P:UDP-glucose catabolic process; ISO:MGI.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Galactose metabolism; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..379
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169883"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 81
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 97..98
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 173
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 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 188
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 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 334..337
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 339..340
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 CONFLICT 1
FT /note="M -> T (in Ref. 1; AAA37658 and 2; AAA83562)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="G -> D (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="Q -> H (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="Q -> E (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="P -> T (in Ref. 3; AAH10985)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="Missing (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="G -> GPCTLAAHAHYLPPLLGSATV (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> P (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..379
FT /note="AIA -> GSPLLDCDHIRALNLCT (in Ref. 1; AAA37658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 43232 MW; 8BA5C776AF6F2D64 CRC64;
MSHSGADPEQ RQQASEADAM AATFRASEHQ HIRYNPLQDE WVLVSAHRMK RPWQGQVEPQ
LLKTVPRHDP LNPLCPGATR ANGEVNPHYD GTFLFDNDFP ALQPDAPDPG PSDHPLFRAE
AARGVCKVMC FHPWSDVTLP LMSVPEIRAV IDAWASVTEE LGAQYPWVQI FENKGAMMGC
SNPHPHCQVW ASSFLPDIAQ REERSQQTYH SQHGKPLLLE YGHQELLRKE RLVLTSEHWI
VLVPFWAVWP FQTLLLPRRH VRRLPELNPA ERDDLASIMK KLLTKYDNLF ETSFPYSMGW
HGAPTGLKTG ATCDHWQLHA HYYPPLLRSA TVRKFMVGYE MLAQAQRDLT PEQAAERLRA
LPEVHYCLAQ KDKETAAIA
