Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.3: Acid Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.3: Acid Phosphatase Like subgroup sequence (ID 465489)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli 908555 Taxon ID: 1268997 553649706 ESD68141.1 (Genbank) URP
Escherichia coli 907710 Taxon ID: 1268985 553595418 ESD16338.1 (Genbank) URP
Escherichia coli 113302 Taxon ID: 1268977 553579134 ESD00667.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a U9Y1T6 U9Y1T6_ECOLX (TrEMBL)
n/a E1ISE5 E1ISE5_ECOLX (TrEMBL)
n/a E6BM45 E6BM45_ECOLX (TrEMBL)
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Sequence

Length of Enzyme (full-length): 317 | Length of Functional Domain: 237

1       10        20        30        40        50        60

MQRIHHNKRKINVSLHRVINIFYTKKDRNVFTGLNIIILLFITKTADNPSFPRQLALWSD
GFCNKSHNKKFQHTDYLGKNMRKITQAISAVCLLFALNSSAVALASSPSPLNPGTNVARL
AEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPV
FWEKMNNGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPVT
NMNPVIFAGDKPGQNTKSQWLQDKNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKP
LPQAGAFGEEVIVNSEY
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
149 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ISS PubMed:17570338
151 Asp (D) side chain Mg2+ ligand; general acid during step 1; base during step 2 metal ligand -- binding,
proton relay -- reactant 		ISS PubMed:17570338
217 Thr (T) side chain None -- ISS PubMed:17570338
257 Lys (K) side chain Facilitates nucleophilic attack by rendering phosphorous center electron deficient electrostatic stabiliser -- spectator IME PubMed:17570338
272 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:17570338
276 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, 2:37 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.