1HXP
NUCLEOTIDE TRANSFERASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004335 | molecular_function | galactokinase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006012 | biological_process | galactose metabolic process |
A | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0004335 | molecular_function | galactokinase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006012 | biological_process | galactose metabolic process |
B | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
B | 0008198 | molecular_function | ferrous iron binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 350 |
Chain | Residue |
A | CYS52 |
A | CYS55 |
A | HIS115 |
A | HIS164 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE A 351 |
Chain | Residue |
A | GLU182 |
A | HIS281 |
A | HIS296 |
A | HIS298 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 349 |
Chain | Residue |
B | CYS52 |
B | CYS55 |
B | HIS115 |
B | HIS164 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE B 350 |
Chain | Residue |
B | GLU182 |
B | HIS281 |
B | HIS296 |
B | HIS298 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME A 352 |
Chain | Residue |
A | CYS99 |
A | HOH567 |
B | PHE4 |
B | PRO6 |
B | HIS11 |
B | TYR225 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 353 |
Chain | Residue |
A | ASN153 |
A | CYS160 |
A | GLN168 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME A 354 |
Chain | Residue |
A | CYS272 |
A | SER273 |
A | PRO275 |
A | LEU303 |
A | ALA307 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE U5P A 355 |
Chain | Residue |
A | PHE53 |
A | ARG60 |
A | VAL61 |
A | PHE75 |
A | ASN77 |
A | ASP78 |
A | PHE79 |
A | HOH586 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 351 |
Chain | Residue |
B | ASN153 |
B | CYS160 |
B | HIS166 |
B | GLN168 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE UDP B 352 |
Chain | Residue |
A | ARG31 |
B | ARG60 |
B | VAL61 |
B | PHE75 |
B | ASN77 |
B | ASP78 |
B | PHE79 |
B | SER161 |
B | ASN162 |
B | HOH355 |
site_id | FR2 |
Number of Residues | 4 |
Details | IRON BINDING SITE |
Chain | Residue |
B | GLU182 |
B | HIS281 |
B | HIS296 |
B | HIS298 |
site_id | FRN |
Number of Residues | 4 |
Details | IRON BINDING SITE |
Chain | Residue |
A | GLU182 |
A | HIS281 |
A | HIS296 |
A | HIS298 |
site_id | NU2 |
Number of Residues | 9 |
Details | NUCLEOTIDE BINDING SITE |
Chain | Residue |
B | LEU54 |
B | VAL61 |
B | PHE75 |
B | ASN77 |
B | ASP78 |
B | PHE79 |
B | VAL108 |
B | SER161 |
B | ASN162 |
site_id | NUC |
Number of Residues | 9 |
Details | NUCLEOTIDE BINDING SITE |
Chain | Residue |
A | LEU54 |
A | VAL61 |
A | PHE75 |
A | ASN77 |
A | ASP78 |
A | PHE79 |
A | VAL108 |
A | SER161 |
A | ASN162 |
site_id | ZN2 |
Number of Residues | 4 |
Details | ZINC BINDING SITE |
Chain | Residue |
B | CYS52 |
B | CYS55 |
B | HIS115 |
B | HIS164 |
site_id | ZNC |
Number of Residues | 4 |
Details | ZINC BINDING SITE |
Chain | Residue |
A | CYS52 |
A | CYS55 |
A | HIS115 |
A | HIS164 |
Functional Information from PROSITE/UniProt
site_id | PS00117 |
Number of Residues | 18 |
Details | GAL_P_UDP_TRANSF_I Galactose-1-phosphate uridyl transferase family 1 active site signature. FENKGaamGcsnpHPHgQ |
Chain | Residue | Details |
A | PHE151-GLN168 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Tele-UMP-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10033, ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869 |
Chain | Residue | Details |
A | HIS166 | |
B | HIS166 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ |
Chain | Residue | Details |
A | ARG28 | |
A | LYS311 | |
A | TYR316 | |
B | ARG28 | |
B | LYS311 | |
B | TYR316 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ, ECO:0007744|PDB:1HXQ |
Chain | Residue | Details |
A | CYS52 | |
B | CYS55 | |
B | HIS115 | |
B | HIS164 | |
B | GLU182 | |
B | HIS281 | |
B | HIS296 | |
B | HIS298 | |
A | CYS55 | |
A | HIS115 | |
A | HIS164 | |
A | GLU182 | |
A | HIS281 | |
A | HIS296 | |
A | HIS298 | |
B | CYS52 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ |
Chain | Residue | Details |
A | VAL61 | |
B | GLY159 | |
B | GLN168 | |
B | GLN323 | |
A | ASN77 | |
A | ASN153 | |
A | GLY159 | |
A | GLN168 | |
A | GLN323 | |
B | VAL61 | |
B | ASN77 | |
B | ASN153 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1hxq |
Chain | Residue | Details |
A | HIS164 | |
A | HIS166 | |
A | CYS160 | |
A | GLN168 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1hxq |
Chain | Residue | Details |
B | HIS164 | |
B | HIS166 | |
B | CYS160 | |
B | GLN168 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 88 |
Chain | Residue | Details |
A | CYS52 | metal ligand |
A | CYS55 | metal ligand |
A | HIS115 | metal ligand |
A | ASN153 | activator, hydrogen bond donor |
A | SER161 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | HIS164 | activator |
A | HIS166 | hydrogen bond donor, nucleofuge, nucleophile |
A | GLN168 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 88 |
Chain | Residue | Details |
B | CYS52 | metal ligand |
B | CYS55 | metal ligand |
B | HIS115 | metal ligand |
B | ASN153 | activator, hydrogen bond donor |
B | SER161 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | HIS164 | activator |
B | HIS166 | hydrogen bond donor, nucleofuge, nucleophile |
B | GLN168 | electrostatic stabiliser, hydrogen bond donor |