Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.4: PGP Like

  ⌊ FunctionalDomain C2.B.4: PGP Like (ID 105348)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli str. K-12 substr. W3110 Taxon ID: 316407 1580717

Uniprot

Protein NameAccessionEC Number Identifier
HMP-PP phosphatase {ECO:0000255|HAMAP-Rule:MF_01847} P46891 COF_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 272 | Length of Functional Domain: 264

1       10        20        30        40        50        60

MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHALEMQHILGALSLDA
YLITGNGTRVHSLEGELLHRDDLPADVAELVLYQQWDTRASMHIFNDDGWFTGKEIPALL
QAFVYSGFRYQIIDVKKMPLGSVTKICFCGDHDDLTRLQIQLYEALGERAHLSFSATDCL
EVLPVGCNKGAALTVLTQHLGLSLRDCMAFGDAMNDREMLVSVGSGFIMGNAMPQLRAEL
PHLPVIGHCRNQAVSHYLTHWLDYPHLPYSPE
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 1/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
42 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:14555659
10 Asp (D) side chain general acid, sometimes general base, Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ISS
189 Lys (K) side chain Binds phosphate, increasing electrophilicity of phosphorous for nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:14555659
212 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659
216 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659

Catalyzed Reaction

HMP-PP phosphatase

+ +
4-amino-2-methyl-5-diphosphonatomethylpyrimidine(3-)
57841		 water
15377		 4-amino-2-methyl-5-phosphonatomethylpyrimidine(2-)
58354		 dihydrogenphosphate
39745

EC: 3.1.3.- | IntEnz: 3.1.3.- | Kegg: 3.1.3.- | BioCyc: 3.1.3.- | BRENDA: 3.1.3.- |

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 7:15 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 261 264
EC number assigned by UniProtKB accession ID.