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Database: UniProt
Entry: F7HA02_MACMU
LinkDB: F7HA02_MACMU
Original site: F7HA02_MACMU 
ID   F7HA02_MACMU            Unreviewed;       379 AA.
AC   F7HA02; G7NFL1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|RuleBase:RU000506};
DE            EC=2.7.7.12 {ECO:0000256|RuleBase:RU000506};
GN   Name=GALT {ECO:0000313|EMBL:AFI34163.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000068509.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFI34163.1};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFI34163.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE77626.1}, Testis
RC   {ECO:0000313|EMBL:AFI34163.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH28967.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000068509.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000068509.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001107,
CC         ECO:0000256|RuleBase:RU000506};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000808-4};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR000808-4};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU000506}.
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC       type 1 family. {ECO:0000256|ARBA:ARBA00010951,
CC       ECO:0000256|RuleBase:RU000506}.
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DR   EMBL; JU333871; AFE77626.1; -; mRNA.
DR   EMBL; JU472163; AFH28967.1; -; mRNA.
DR   EMBL; JV044092; AFI34163.1; -; mRNA.
DR   PaxDb; 9544-ENSMMUP00000027360; -.
DR   Ensembl; ENSMMUT00000100498.1; ENSMMUP00000068509.1; ENSMMUG00000048888.2.
DR   VEuPathDB; HostDB:ENSMMUG00000048888; -.
DR   GeneTree; ENSGT00940000160904; -.
DR   HOGENOM; CLU_029960_0_0_1; -.
DR   OrthoDB; 1428870at2759; -.
DR   TreeFam; TF300018; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000006718; Chromosome 15.
DR   Bgee; ENSMMUG00000048888; Expressed in ileum and 21 other cell types or tissues.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:InterPro.
DR   CDD; cd00608; GalT; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 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   NCBIfam; TIGR00209; galT_1; 1.
DR   PANTHER; PTHR11943; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR11943:SF1; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF02744; GalP_UDP_tr_C; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF000808; GalT; 1.
DR   SUPFAM; SSF54197; HIT-like; 2.
DR   PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000506};
KW   Galactose metabolism {ECO:0000256|RuleBase:RU000506};
KW   Iron {ECO:0000256|PIRSR:PIRSR000808-4};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000808-4};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          23..196
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          203..368
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT   BINDING         48..51
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
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:0000256|PIRSR:PIRSR000808-2"
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:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         173
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:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         179..181
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:0000256|PIRSR:PIRSR000808-2"
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:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         319
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         321
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         334..335
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
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                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         346
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:0000256|PIRSR:PIRSR000808-2"
SQ   SEQUENCE   379 AA;  43257 MW;  FE2D04A066A7BF0B CRC64;
     MSRSGTDPEQ RQQASEADAA AATFRASDHQ HIRYNPLQDE WVLVSAHRMK RPWQGQVEPQ
     LLKTVPRHDP LNPLCPGATR ANGEVNPHYD STFLFDNDFP ALQPDAPSPG PSDHPLFQAK
     AARGVCKVMC FHPWSDVTLP LMSVPEIRAV VDAWASVTEE LGAQYPWVQI FENKGAMMGC
     SNPHPHCQVW ASSFLPDIAQ REERSQQTYK SQHGEPLLME YSRQELLRKE RLVLTSEHWL
     VLVPFWATWP YQTLLLPRRH VQRLPELTPA ERDDLASIMK KLLTKYDNLF ETSFPYSMGW
     HGAPTGSEAG ANWDHWQLHA HYYPPLLRSA TVRKFMVGYE MLAQAQRDLT PEQAAERLRA
     LPDVHYSLGQ KDRETATIA
//
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