Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.6: Phosphoserine Phosphatase Like

  ⌊ C1.6.2: Deoxy-d-mannose-octulosonate 8-phosphate Phosphatase Like

     ⌊ Family deoxy-d-mannose-octulosonate 8-phosphate phosphatase

  ⌊ FunctionalDomain deoxy-d-mannose-octulosonate 8-phosphate phosphatase (ID 2351)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:12639950
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Haemophilus influenzae Rd KW20 Taxon ID: 71421 20150364 PRP URP
Haemophilus influenzae Rd KW20 Taxon ID: 71421 20150363 PRP URP
Haemophilus influenzae Rd KW20 Taxon ID: 71421 20150362 PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC P45314 3.1.3.45 KDSC_HAEIN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 180 | Length of Functional Domain: 172

1       10        20        30        40        50        60

XQQKLENIKFVITDVDGVLTDGQLHYDANGEAIKSFHVRDGLGIKXLXDADIQVAVLSGR
DSPILRRRIADLGIKLFFLGKLEKETACFDLXKQAGVTAEQTAYIGDDSVDLPAFAACGT
SFAVADAPIYVKNAVDHVLSTHGGKGAFREXSDXILQAQGKSSVFDTAQGFLKSVKSXGQ
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
58 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
14 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ISS PubMed:11835514
16 Asp (D) side chain Mg2+ ligand, general acid: donates proton to leaving group, general base: activates water metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:11835514
58 Ser (S) side chain binds phosphate moiety of substrate, positions water steric role -- spectator,
substrate binding -- binding 		ICS PubMed:11835514
84 Lys (K) side chain positions nucleophilic Asp, binds phosphate moiety of substrate steric role -- spectator,
substrate binding -- binding 		ICS PubMed:11835514
107 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:11835514
111 Asp (D) side chain positions Lys steric role -- spectator ICS PubMed:11835514
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
14 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ISS PubMed:11835514
16 Asp (D) side chain Mg2+ ligand, general acid: donates proton to leaving group, general base: activates water metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:11835514
58 Ser (S) side chain binds phosphate moiety of substrate, positions water steric role -- spectator,
substrate binding -- binding 		ICS PubMed:11835514
84 Lys (K) side chain positions D28, binds phosphate moiety of substrate steric role -- spectator,
substrate binding -- binding 		ICS PubMed:11835514
107 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:11835514
111 Asp (D) side chain positions K98 steric role -- spectator ICS PubMed:11835514

Catalyzed Reaction

3-deoxy-manno-octulosonate-8-phosphatase

+ +
8-phosphonato-3-deoxy-D-manno-oct-2-ulosonate(3-)
58368		 water
15377		 keto-3-deoxy-D-manno-octulosonate
16064		 hydrogenphosphate
43474

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1K1E Structure Of The Cobalt-Bound Form Of The Deoxy-D-Mannose-Octulosonate 8-Phosphate Phosphatase (Yrbi) From Haemophilus Influenzae (Hi1679) Deoxy-D-Mannose-Octulosonate 8-Phosphate Phosphatase 20 1.67 Cobalt (Ii) Ion
(4 more ⇓) 		CSA • PDB • PDBSum
1J8D Structure Of The Metal-Free Form Of The Deoxy-D-Mannose-Octulosonate 8-Phosphate Phosphatase (Yrbi) From Haemophilus Influenzae (Hi1679) Deoxy-D-Mannose-Octulosonate 8-Phosphate Phosphatase 11 2.3 Selenomethionine • Glycerol CSA • PDB • PDBSum
4HGP Crystal Structure Of 2-Keto-3-Deoxyoctulosonate 8-Phosphate Phosphohydrolase From Haemophilus Influenzae In Complex With Transition State Mimic 3-Deoxy-D-Manno-Octulosonate 8-Phosphate Phosphatase Kdsc 20 1.8 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.