ID D8I9Y3_BRAP9 Unreviewed; 332 AA.
AC D8I9Y3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000313|EMBL:ADK30100.1};
GN Name=galT {ECO:0000313|EMBL:ADK30100.1};
GN OrderedLocusNames=BP951000_0091 {ECO:0000313|EMBL:ADK30100.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30100.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK30100.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
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 -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000256|ARBA:ARBA00010951}.
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DR EMBL; CP002025; ADK30100.1; -; Genomic_DNA.
DR RefSeq; WP_013243055.1; NC_014330.1.
DR AlphaFoldDB; D8I9Y3; -.
DR STRING; 759914.BP951000_0091; -.
DR GeneID; 56438681; -.
DR KEGG; bpo:BP951000_0091; -.
DR eggNOG; COG1085; Bacteria.
DR HOGENOM; CLU_029960_1_0_12; -.
DR InParanoid; D8I9Y3; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000332; Chromosome.
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 Gene3D; 3.30.428.10; HIT-like; 2.
DR InterPro; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR005850; GalP_Utransf_C.
DR InterPro; IPR005849; GalP_Utransf_N.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR42763; ADP-GLUCOSE PHOSPHORYLASE; 1.
DR PANTHER; PTHR42763:SF2; ADP-GLUCOSE PHOSPHORYLASE; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000808-3};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ADK30100.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000332};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADK30100.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT DOMAIN 2..175
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 187..281
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
FT ACT_SITE 165
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
SQ SEQUENCE 332 AA; 38276 MW; 6A075F0A34FE5DB0 CRC64;
MPHIRKDPVT KQSVIIASER MGRPSDYINI EEKHAILSSD NTCPFCKGNE DKTPEHSTII
FDDNKNWIVR IVPNKYPIIA QSNADELPEK NSLFEADICK GFHDVIIENP NHSFNYYNAE
ERDLFFIFEA IIMRFQELSK EKDMMYSLLF KNFGREAGAS LVHSHAQMMT TPFVPIQIME
EIYGSLEYYN ENKKCVYCSM IEEEKKINER VICENNDFIA ISPFASKSPY QIYILPKKHS
DSIVYSEDCI SQFASIVKDI FNRINKVLGE ISFNYVLHTL TPALEKKYSH SSHWFLDIMP
KMSKLAGYEL GSGVFINSIT PEDATNDLKN AL
//
