Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.1: Sucrose Phosphatase Like

  ⌊ FunctionalDomain C2.B.1: Sucrose Phosphatase Like (ID 37106)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Agrobacterium tumefaciens str. C58 Taxon ID: 176299 15888002 NP_353683.1 (RefSeq) URP
Taxon ID: 1183400 499273654 WP_010971047.1 (RefSeq)
n/a 756456435 AJL50865.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Mannosylfructose-phosphate phosphatase {ECO:0000312|EMBL:ABU63293.1} A9CK30 3.1.3.79 MFPP_AGRFC (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 248 | Length of Functional Domain: 248

1       10        20        30        40        50        60

MKPLRLLSTDLDGTVVGDNDATRRFRDFWHALPDDLRPVLVFNSGRLIDDQLALLEEVPL
PQPDYIIGGVGTMLHAKKRSELETAYTQSLGTGFDPRKIADVMNRIAGVTMQEERYQHGL
KSSWFLHDADAAALGEIEAALLAADIDARIVYSSDRDLDILPKAADKGAALAWLCGQLRI
GLDESVVSGDTGNDRAMFELKTIRGVIVGNALPELVSLAHQDNRFFHSTAKEADGVIEGL
RHWGLNPR
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
10 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
12 Asp (D) side chain Mg2+ ligand, binds and orients phosphate group metal ligand -- binding,
steric role -- spectator 		ICS PubMed:15937230
44 Ser (S) side chain Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
167 Lys (K) side chain Orients Asp nucleophile, Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
190 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15937230
194 Asp (D) side chain Mg2+ ligand when metal in noncatalytic position metal ligand -- binding ICS PubMed:15937230

Catalyzed Reaction

mannosylfructose-phosphate phosphatase

+ +
beta-D-fructofuranosyl alpha-D-mannopyranoside 6(F)-phosphate
51834		 water
15377		 beta-D-fructofuranosyl alpha-D-mannopyranoside
51833		 phosphoric acid
26078

EC: 3.1.3.79 | IntEnz: 3.1.3.79 | Kegg: 3.1.3.79 | BioCyc: 3.1.3.79 | BRENDA: 3.1.3.79

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 11:25 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.