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Database: UniProt
Entry: M1VA74_CYAM1
LinkDB: M1VA74_CYAM1
Original site: M1VA74_CYAM1 
ID   M1VA74_CYAM1            Unreviewed;       359 AA.
AC   M1VA74;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|RuleBase:RU000506};
DE            EC=2.7.7.12 {ECO:0000256|RuleBase:RU000506};
GN   ORFNames=CYME_CMQ030C {ECO:0000313|EMBL:BAM81964.1};
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM81964.1, ECO:0000313|Proteomes:UP000007014};
RN   [1] {ECO:0000313|EMBL:BAM81964.1, ECO:0000313|Proteomes:UP000007014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10D {ECO:0000313|EMBL:BAM81964.1,
RC   ECO:0000313|Proteomes:UP000007014};
RX   PubMed=15071595; DOI=10.1038/nature02398;
RA   Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA   Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA   Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA   Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA   Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA   Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA   Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA   Kuroiwa T.;
RT   "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT   merolae 10D.";
RL   Nature 428:653-657(2004).
RN   [2] {ECO:0000313|EMBL:BAM81964.1, ECO:0000313|Proteomes:UP000007014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10D {ECO:0000313|EMBL:BAM81964.1,
RC   ECO:0000313|Proteomes:UP000007014};
RX   PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA   Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA   Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA   Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT   "A 100%-complete sequence reveals unusually simple genomic features in the
RT   hot-spring red alga Cyanidioschyzon merolae.";
RL   BMC Biol. 5:28-28(2007).
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|PIRSR:PIRSR000808-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000808-3};
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; AP006499; BAM81964.1; -; Genomic_DNA.
DR   RefSeq; XP_005538000.1; XM_005537943.1.
DR   AlphaFoldDB; M1VA74; -.
DR   SMR; M1VA74; -.
DR   STRING; 280699.M1VA74; -.
DR   EnsemblPlants; CMQ030CT; CMQ030CT; CMQ030C.
DR   GeneID; 16996397; -.
DR   Gramene; CMQ030CT; CMQ030CT; CMQ030C.
DR   KEGG; cme:CYME_CMQ030C; -.
DR   eggNOG; KOG2958; Eukaryota.
DR   HOGENOM; CLU_029960_0_0_1; -.
DR   OMA; CFENRGA; -.
DR   OrthoDB; 1428870at2759; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000007014; Chromosome 17.
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   3: Inferred from homology;
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:PIRSR000808-3};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007014};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT   DOMAIN          4..186
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          193..358
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
FT   ACT_SITE        176
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT   BINDING         28..31
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         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
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:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         78..79
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         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         163
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         169..171
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         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         178
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         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         292
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         325..326
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         330..331
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         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:0000256|PIRSR:PIRSR000808-2"
SQ   SEQUENCE   359 AA;  40572 MW;  35CD2ED583F8A7C5 CRC64;
     MASFDFTEHP HRRFNPLKGE WVLCSPHRAK RPWQGAQETV GGEERPRYDP ECYLCPGNTR
     AGGAHRNPQY DATFVFTNDF PALLLDGPSD SADAEASRAS HATLFQARPV SGTCRVVCFS
     PRHDLTLAEM SRSEIRRVVD AWQEQYAELA TMPQIRHVQI FENKGSAMGC SNPHPHGQIW
     ASSFIPNEIA TELRLQSAYY ADTGRELLLD YLKAELQRPN ERIVCQNPHF VALVPFWAVW
     PFEVMVLPTG SCQSLLDIDA SQKDDLADIL QRVTVRYDNL FKTSFPYSMG LHQAPVANGA
     ATAEPGLLFH IHFYPPLLRS ATVRKFMVGF EMLAESQRDL TAEQAAERLR SLPEKHYRA
//
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