Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.1: Acid Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.1: Acid Phosphatase Like subgroup sequence (ID 468630)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Haemophilus sp. oral taxon 851 Taxon ID: 762964 497184334 WP_009500702.1 (RefSeq)
Haemophilus sp. oral taxon 851 str. F0397 Taxon ID: 762965 371758068 EHO46845.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a H1LQ49 H1LQ49_9PAST (TrEMBL)

Sequence

Length of Enzyme (full-length): 274 | Length of Functional Domain: 232

1       10        20        30        40        50        60

MKTTLKMTALAALSAFVLAGCGSHQMKSEDHAKMQLQQQAVLGLNWMQDSGEYKALAYQA
YNAAKVAFDHAKVAKGKKKAVVVDLDETMLDNSPYAGWQVQNNKPFDGKDWTRWVDARQS
RAVPGAVEFNNYVNSHKGKMFYVTNRKDSTEKAGTIDDMKRLGFNGVEESAFYLKKDKSA
KAARFAEIEKQGYEIVLYVGDNLDDFGDTVYGKLNADRRAFVDQNQGKFGKTFIMLPNAN
YGGWEGGLADGYFKKDTQGKIKARLDAVQAWDGK
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

Subgroup CAR This EFD conserves 8/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
84 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:17824671
86 Asp (D) side chain general acid (donates proton to leaving group); Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20934434
111 Trp (W) side chain aromatic box (binds sbst) substrate binding -- binding ICS PubMed:20934434
144 Thr (T) side chain stabilizes substrate phosphoryl group electrostatic stabiliser -- spectator ICS PubMed:17824671
181 Lys (K) side chain stabilizes substrate phosphoryl group electrostatic stabiliser -- spectator ICS PubMed:17824671
201 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:17824671
205 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:17824671
241 Tyr (Y) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:17824671

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3ET4 Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Outer Membrane Protein P4, Nadp Phosphatase 23 1.7 Magnesium Ion • Tetraethylene Glycol CSA • PDB • PDBSum
3ET5 Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed With Tungstate Outer Membrane Protein P4, Nadp Phosphatase 23 2.0 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
3OCZ Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed With The Inhibitor Adenosine 5-O-Thiomonophosphate Lipoprotein E 23 1.35 Magnesium Ion • Adenosine -5'-Thio-Monophosphate CSA • PDB • PDBSum
3OCY Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed With Inorganic Phosphate Lipoprotein E 23 1.4 Phosphate Ion • Magnesium Ion CSA • PDB • PDBSum
3SF0 Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed With 5'Amp Lipoprotein E 23 1.35 Yes Magnesium Ion • Adenosine Monophosphate CSA • PDB • PDBSum
3OCW Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed With 3'-Amp Lipoprotein E 23 1.85 Yes Magnesium Ion • [(2R,3S,4R,5R)-5-(6-Aminopurin-9-Yl)-4-Hydroxy-2-(Hydroxymethyl)Oxolan-3-Yl] Dihydrogen Phosphate CSA • PDB • PDBSum
3OCV Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed With 5'-Amp Lipoprotein E 23 1.55 Yes Adenosine Monophosphate • Magnesium Ion CSA • PDB • PDBSum
3OCU Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed With Nmn Lipoprotein E 23 1.35 Yes Magnesium Ion • Beta-Nicotinamide Ribose Monophosphate CSA • PDB • PDBSum
3OCX Structure Of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed With 2'-Amp Lipoprotein E 23 1.9 Yes Adenosine-2'-Monophosphate • Magnesium Ion 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
Aug. 1, 2014, 2:52 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.