ID A0A2N1DE97_9ALTE Unreviewed; 349 AA.
AC A0A2N1DE97;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00016340, ECO:0000256|RuleBase:RU000506};
DE EC=2.7.7.12 {ECO:0000256|ARBA:ARBA00012384, ECO:0000256|RuleBase:RU000506};
GN ORFNames=CXF95_04345 {ECO:0000313|EMBL:PKG99894.1};
OS Paraglaciecola sp. MB-3u-78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=2058332 {ECO:0000313|EMBL:PKG99894.1, ECO:0000313|Proteomes:UP000233828};
RN [1] {ECO:0000313|EMBL:PKG99894.1, ECO:0000313|Proteomes:UP000233828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-78 {ECO:0000313|EMBL:PKG99894.1,
RC ECO:0000313|Proteomes:UP000233828};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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=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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKG99894.1}.
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DR EMBL; PJCF01000003; PKG99894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1DE97; -.
DR OrthoDB; 9769064at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000233828; Unassembled WGS sequence.
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 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:UP000233828};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT DOMAIN 3..176
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 185..346
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
FT ACT_SITE 166
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
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 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
SQ SEQUENCE 349 AA; 39377 MW; 562CA41A3B87928C CRC64;
MSKFDPVDHS HRRRNPLTGD WVLVSPHRAK RPWQGQVENP QLADTVPHDP ECFLCSGNTR
INGEVNPEYD GTFVFTNDFA ALMQDTPAAQ QSNDDLFTLQ AARGTSRVIC FSPEHNKTLP
ELSLPALEGV IDTWQEQVAD LSKDYVWVQV FENKGAAMGC SNPHPHGQVW ANDFIPNEVA
KAEASQKAYF EKHASSLLLD YAQRESADSS RTVVETEHWI AVVPYWAAWP FETLLMPKFA
CARLTDVNAA QKADLAIAIK KLTSRYDNLF QCSFPYSMGW HGAPNNLDST EHWQVHAHFY
PPLLRSATVR KFMVGYEMMA EPQRDLTPEQ AAQRLQTLSD VHYNESTGA
//
