GALT_RAT
ID GALT_RAT Reviewed; 379 AA.
AC P43424; Q4KM61;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8400361; DOI=10.3109/10425179309020829;
RA Heidenreich R.A., Mallee J., Segal S.;
RT "Rat galactose-1-phosphate uridyltransferase coding sequence, transcription
RT start site and genomic organization.";
RL DNA Seq. 3:311-318(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
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}.
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DR EMBL; L05541; AAC37609.1; -; Genomic_DNA.
DR EMBL; BC098756; AAH98756.1; -; mRNA.
DR PIR; A56685; A56685.
DR RefSeq; NP_001013107.1; NM_001013089.2.
DR AlphaFoldDB; P43424; -.
DR SMR; P43424; -.
DR STRING; 10116.ENSRNOP00000019886; -.
DR PhosphoSitePlus; P43424; -.
DR PaxDb; P43424; -.
DR PRIDE; P43424; -.
DR GeneID; 298003; -.
DR KEGG; rno:298003; -.
DR UCSC; RGD:1306483; rat.
DR CTD; 2592; -.
DR RGD; 1306483; Galt.
DR VEuPathDB; HostDB:ENSRNOG00000014766; -.
DR eggNOG; KOG2958; Eukaryota.
DR HOGENOM; CLU_029960_0_1_1; -.
DR InParanoid; P43424; -.
DR OMA; HAIYYPP; -.
DR OrthoDB; 1135699at2759; -.
DR PhylomeDB; P43424; -.
DR TreeFam; TF300018; -.
DR BRENDA; 2.7.7.12; 5301.
DR Reactome; R-RNO-70370; Galactose catabolism.
DR SABIO-RK; P43424; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:P43424; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000014766; Expressed in liver and 20 other tissues.
DR Genevisible; P43424; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005534; F:galactose binding; IC:RGD.
DR GO; GO:0005536; F:glucose binding; IC:RGD.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR GO; GO:0006012; P:galactose metabolic process; IDA:RGD.
DR GO; GO:0061623; P:glycolytic process from galactose; ISO:RGD.
DR GO; GO:0006258; P:UDP-glucose catabolic process; IDA:RGD.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISO:RGD.
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 2: Evidence at transcript 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_0000169884"
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"
SQ SEQUENCE 379 AA; 43314 MW; F217FA0A3A3E4665 CRC64;
MSQSGADPEQ RQQASEADAM AATFRASEHQ HIRYNPLQDE WVLVSAHRMK RPWQGQVEPQ
LLKTVPRHDP LNPLCPGATR ANGEVNPPYD GTFLFDNDFP ALQPDAPDPG PSDHPLFRVE
AARGVCKVMC FHPWSDVTLP LMSVPEIRAV IDAWASVTEE LGAQYPWVQI FENKGAMMGC
SNPHPHCQVW ASNFLPDIAQ REERSQQTYH NQHGKPLLLE YGHQELLRKE RLVLTSEYWI
VLVPFWAVWP FQTLLLPRRH VQRLPELTPA ERDDLASTMK KLLTKYDNLF ETSFPYSMGW
HGAPMGLKTG ATCDHWQLHA HYYPPLLRSA TVRKFMVGYE MLAQAQRDLT PEQAAERLRV
LPEVHYCLTQ KDKETAATA
