Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.1: Sucrose Phosphatase Like

     ⌊ Family sucrose-phosphatase

  ⌊ FunctionalDomain sucrose-phosphatase (ID 2232)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Synechocystis sp. PCC 6803 Taxon ID: 1148 499175453 WP_010873040.1 (RefSeq) URP
n/a 756456424 AJL50854.1 (Genbank)
n/a 756455147 AJL49577.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q7BII3 Q7BII3_9SYNC (TrEMBL)
n/a P74325 P74325_SYNY3 (TrEMBL)
n/a L8ATN1 L8ATN1_BACIU (TrEMBL)

Sequence

Length of Enzyme (full-length): 244 | Length of Functional Domain: 243

1       10        20        30        40        50        60

MRQLLLISDLDNTWVGDQQALEHLQEYLGDRRGNFYLAYATGRSYHSARELQKQVGLMEP
DYWLTAVGSEIYHPEGLDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYH
LDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQ
TLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAILEAIAHF
DFLS
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
9 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15937230
11 Asp (D) side chain Mg2+ ligand, binds and orients phosphate group metal ligand -- binding,
steric role -- spectator 		ICS PubMed:15937230
41 Thr (T) side chain Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
163 Lys (K) side chain Orients Asp nucleophile, Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
186 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15937230
190 Asp (D) side chain Mg2+ ligand when metal in noncatalytic position metal ligand -- binding ICS PubMed:15937230
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15937230
11 Asp (D) side chain Mg2+ ligand, binds and orients phosphate group metal ligand -- binding,
steric role -- spectator 		ICS PubMed:15937230
41 Thr (T) side chain Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
163 Lys (K) side chain Orients Asp nucleophile, Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
186 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15937230
190 Asp (D) side chain Mg2+ ligand when metal in "noncatalytic" position metal ligand -- binding ICS PubMed:15937230

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1TJ3 X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 In A Closed Conformation Sucrose-Phosphatase 1 2.8 Magnesium Ion CSA • PDB • PDBSum
1TJ5 X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 In Complex With Sucrose And Phosphate Sucrose-Phosphatase 1 2.2 Sucrose
(2 more ⇓) 		CSA • PDB • PDBSum
1TJ4 X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 In Complex With Sucrose Sucrose-Phosphatase 1 2.7 Sucrose • Magnesium Ion CSA • PDB • PDBSum
1U2T X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 In Complex With Sucrose6P Sucrose-Phosphatase (Spp) 1 2.9 Sucrose-6-Phoshpate CSA • PDB • PDBSum
2B1R X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp.Pcc6803 In Complex With Cellobiose Hypothetical Protein Slr0953 1 2.2 Cellobiose • Magnesium Ion CSA • PDB • PDBSum
2B1Q X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp.Pcc6803 In Complex With Trehalose Hypothetical Protein Slr0953 1 2.2 Magnesium Ion • Trehalose CSA • PDB • PDBSum
1U2S X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 In Complex With Glucose Sucrose-Phosphatase 1 2.5 Alpha-D-Glucose • Magnesium Ion CSA • PDB • PDBSum
1S2O X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp. Pcc6803 At 1.40 A Resolution Sucrose-Phosphatase 1 1.4 Magnesium Ion CSA • PDB • PDBSum
2D2V X-Ray Structure Of The Sucrose-Phosphatase (Spp) From Synechocystis Sp.Pcc6803 In Complex With Maltose Hypothetical Protein Slr0953 1 2.5 Maltose • 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
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.