ID C5S1G9_9PAST Unreviewed; 349 AA.
AC C5S1G9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
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=AM305_08736 {ECO:0000313|EMBL:EER47246.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47246.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER47246.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER47246.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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}.
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:EER47246.1}.
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DR EMBL; ACQL01000086; EER47246.1; -; Genomic_DNA.
DR RefSeq; WP_005823656.1; NZ_ACQL01000086.1.
DR AlphaFoldDB; C5S1G9; -.
DR eggNOG; COG1085; Bacteria.
DR OrthoDB; 9769064at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000005532; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT DOMAIN 5..177
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 184..348
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
FT ACT_SITE 167
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT BINDING 283
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
SQ SEQUENCE 349 AA; 40588 MW; 77A5B529F57BD470 CRC64;
MTTQFILNDH PHRRFNPLKN QWILVSPHRA KRPWQGQQEE IVAEDKPSYD PTCYLCPSNK
RITGEQNPAY SKPFVFKNDF SALLPDTPAP EANDDPLFQI SHTQGESRVI CFSPDHSKTL
PQLSVEEISQ VVDVWQEQVG ELKQRYQWVQ LFENKGAMMG CSNPHPHGQI WASNFLPNEL
ATEDECQADY FAKHQRPLLL DYAQRELEKK ERIVVETKDW IAVVPYWAAW PFETLLLPKA
KQFKSIEELN PAEKEDLALA LKKLTTRYDN LFNISFPYSM GFHFAPFNGK ENAHWQLHAH
FYPPLLRSAT VRKFMVGYEM MAESQRDLTP EQAAERLNAV SDEVHYKDK
//
