Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.3: Acid Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.3: Acid Phosphatase Like subgroup sequence (ID 478925)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 543 446190301 WP_000268156.1 (RefSeq)
Escherichia coli 5-366-08_S4_C1 Taxon ID: 1444212 660333327 KEO20795.1 (Genbank) URP
Escherichia coli 2-222-05_S3_C2 Taxon ID: 1444153 660305550 KEN94010.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Class B acid phosphatase P0AE22 3.1.3.2 APHA_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 174 | Length of Functional Domain: 174

1       10        20        30        40        50        60

MAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVARQLI
DMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQWLQD
KNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY
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 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
6 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ISS PubMed:17570338
8 Asp (D) side chain Mg2+ ligand; general acid during step 1; base during step 2 metal ligand -- binding,
proton relay -- reactant 		ISS PubMed:17570338
74 Thr (T) side chain None -- ISS PubMed:17570338
114 Lys (K) side chain Facilitates nucleophilic attack by rendering phosphorous center electron deficient electrostatic stabiliser -- spectator IME PubMed:17570338
129 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:17570338
133 Asp (D) side chain Interacts with catalytic Lys and loop 4 -- structural ICS PubMed:17570338

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2B82 Crystal Structure Of Apha Class B Acid Phosphatase/Phosphotransferase Ternary Complex With Adenosine And Phosphate Bound To The Catalytic Metal At 1.2 A Resolution Class B Acid Phosphatase 62 1.25 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
2B8J Crystal Structure Of Apha Class B Acid Phosphatase/Phosphotransferase Ternary Complex With Adenosine And Phosphate At 2 A Resolution Class B Acid Phosphatase 62 2.03 Magnesium Ion
(5 more ⇓) 		CSA • PDB • PDBSum
2HF7 Transition State Analogue Of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex) Class B Acid Phosphatase 62 1.6 Magnesium Ion • Aluminum Fluoride CSA • PDB • PDBSum
2G1A Crystal Structure Of The Complex Between Apha Class B Acid Phosphatase/Phosphotransferase Class B Acid Phosphatase 62 2.0 Magnesium Ion • {[2-(6-Amino-9H-Purin-9-Yl)Ethoxy]Methyl}Phosphonic Acid CSA • PDB • PDBSum
1N9K Crystal Structure Of The Bromide Adduct Of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli At 2.2 A Resolution Class B Acid Phosphatase 62 2.2 Magnesium Ion • Bromide Ion CSA • PDB • PDBSum
1N8N Crystal Structure Of The Au3+ Complex Of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli At 1.69 A Resolution Class B Acid Phosphatase 62 1.69 Gold 3+ Ion CSA • PDB • PDBSum
3CZ4 Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli Class B Acid Phosphatase 62 1.7 Magnesium Ion
(3 more ⇓) 		CSA • PDB • PDBSum
1RMY Crystal Structure Of Apha Class B Acid Phosphatase/Phosphotransferase Ternary Complex With Deoxycytosine And Phosphate Bound To The Catalytic Metal Class B Acid Phosphatase 62 1.75 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
1RMT Crystal Structure Of Apha Class B Acid Phosphatase/Phosphotransferase Complexed With Adenosine. Class B Acid Phosphatase 62 1.4 Magnesium Ion • Adenosine CSA • PDB • PDBSum
1RMQ Crystal Structure Of Apha Class B Acid Phosphatase/Phosphotransferase With Osmiate Mimicking The Catalytic Intermediate Class B Acid Phosphatase 62 2.0 Cobalt (Ii) Ion • Osmium Ion CSA • PDB • PDBSum
2HEG Phospho-Aspartyl Intermediate Analogue Of Apha Class B Acid Phosphatase/Phosphotransferase Class B Acid Phosphatase 62 1.5 Aspartate Beryllium Trifluoride • 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, 3:54 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.