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Database: UniProt
Entry: C0M8Y5_STRE4
LinkDB: C0M8Y5_STRE4
Original site: C0M8Y5_STRE4 
ID   C0M8Y5_STRE4            Unreviewed;       494 AA.
AC   C0M8Y5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE            Short=Gal-1-P uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE            EC=2.7.7.12 {ECO:0000256|HAMAP-Rule:MF_00571};
DE   AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
GN   Name=galT {ECO:0000256|HAMAP-Rule:MF_00571};
GN   OrderedLocusNames=SEQ_1963 {ECO:0000313|EMBL:CAW95200.1};
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW95200.1, ECO:0000313|Proteomes:UP000001365};
RN   [1] {ECO:0000313|EMBL:CAW95200.1, ECO:0000313|Proteomes:UP000001365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047 {ECO:0000313|EMBL:CAW95200.1,
RC   ECO:0000313|Proteomes:UP000001365};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00571};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|HAMAP-Rule:MF_00571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00571}.
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC       type 2 family. {ECO:0000256|ARBA:ARBA00008706, ECO:0000256|HAMAP-
CC       Rule:MF_00571}.
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DR   EMBL; FM204883; CAW95200.1; -; Genomic_DNA.
DR   RefSeq; WP_012680122.1; NC_012471.1.
DR   AlphaFoldDB; C0M8Y5; -.
DR   KEGG; seu:SEQ_1963; -.
DR   HOGENOM; CLU_047799_0_0_9; -.
DR   OrthoDB; 2293at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000001365; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00571; GalP_UDP_trans; 1.
DR   InterPro; IPR000766; GalP_uridyl_Trfase_II.
DR   InterPro; IPR023425; GalP_uridyl_Trfase_II_CS.
DR   InterPro; IPR005850; GalP_Utransf_C.
DR   InterPro; IPR005849; GalP_Utransf_N.
DR   NCBIfam; TIGR01239; galT_2; 1.
DR   PANTHER; PTHR39191:SF1; DUF4922 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR39191; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF02744; GalP_UDP_tr_C; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF006005; GalT_BS; 1.
DR   PROSITE; PS01163; GAL_P_UDP_TRANSF_II; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00571};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00571};
KW   Galactose metabolism {ECO:0000256|ARBA:ARBA00023144, ECO:0000256|HAMAP-
KW   Rule:MF_00571};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00571};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00571}.
FT   DOMAIN          17..225
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          241..434
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
SQ   SEQUENCE   494 AA;  56024 MW;  2191A4A88F87FC0D CRC64;
     MASLIDTFVR KVIEHSDYTS EDAIYIRNRV LALVGENHVW QETSLTALIA LKEALVELAA
     ENGKIGRLPE EKDCLGAELM NMITPIPSVV NRRFWDTYAQ SPQQAISDFY QLSQLNDYIK
     TAAIAKNISF TVPSQYGDMA ITINLSKPEK DPKAIAAAKK AKASSYPKCQ LCMENEGYQG
     RINHPARANH RIIRMSLGNE AWGFQYSPYA YFNEHSIIFN TEHVPMTIST STFRQLLDIV
     DILPDYFVGS NADLPIVGGS ILTHNHYQAG RHVFPMEIAK QDKRFTFKGF PDIQAATLNW
     PMSVIRLRSS NKDQLVQLAD TIRLAWRHYS DDSVDIVAYT NQEPHHTITP IARKKEGQFE
     LDLVLRDNHT SEQFPDGVYH PHADVQHIKK ENIGLIEVMG LAILPPRLKE ELVEVKKYIL
     NQANQIADYH KDWADQITLR PDLSAITVDD IIQEEVGSVF VRVLEDAGVY KRDQEGQAAF
     MRFLKSIGIE AIEE
//
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