Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.3: Acid Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.3: Acid Phosphatase Like subgroup sequence (ID 465961)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 485872024 WP_001468912.1 (RefSeq) URP
Escherichia coli 5-366-08_S1_C1 Taxon ID: 1444047 660076460 KEL71951.1 (Genbank) URP
Escherichia coli 5-366-08_S1_C3 Taxon ID: 1444102 658727749 KEJ68943.1 (Genbank) URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A073GT49 A0A073GT49_ECOLX (TrEMBL)
n/a A0A073UW09 A0A073UW09_ECOLX (TrEMBL)
n/a W1WQ62 W1WQ62_ECOLX (TrEMBL)

Sequence

Length of Enzyme (full-length): 237 | Length of Functional Domain: 237

1       10        20        30        40        50        60

MRKITQAISAVCLLFALNSSAVALASSPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAG
RPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVAR
QLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQW
LQDKNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIINSEY
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
69 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ISS PubMed:17570338
71 Asp (D) side chain Mg2+ ligand; general acid during step 1; base during step 2 metal ligand -- binding,
proton relay -- reactant 		ISS PubMed:17570338
137 Thr (T) side chain None -- ISS PubMed:17570338
177 Lys (K) side chain Facilitates nucleophilic attack by rendering phosphorous center electron deficient electrostatic stabiliser -- spectator IME PubMed:17570338
192 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:17570338
196 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
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
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
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, 2:39 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.