Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.3: Phosphomannomutase Like

  ⌊ FunctionalDomain C2.B.3: Phosphomannomutase Like (ID 276233)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Ailuropoda melanoleuca Taxon ID: 9646 281340936 EFB16520.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a F1PKB3 F1PKB3_CANLF (TrEMBL)
n/a D2I287 D2I287_AILME (TrEMBL)

Sequence

Length of Enzyme (full-length): 234 | Length of Functional Domain: 228

1       10        20        30        40        50        60

QKIDPEVAAFLQKLRSRVQIGVVGGSDYSKIAEQLGEGDEVIEKFDYVFAENGTVQYKHG
RLLSKQTIQNHLGEELLQDLINFCLRYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLE
ERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQD
SFDTIHFFGNETSPGGNDFEIYADPRTVGHSVVSPQDTVQRCREIFFPETAHEA
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
Superfamily CAR This EFD conserves 0/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
24 Gly (G) side chain MISMATCH: This residue does not match the specified amino acid type of S,T, and thus may not function in the same manner as other sequences in the superfamily
Subgroup CAR This EFD conserves 6/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
34 Gln (Q) side chain Positions acid/base Asp steric role -- spectator ICS PubMed:16540464
160 Ser (S) side chain Binds phosphate substrate binding -- binding ICS PubMed:16540464
170 Lys (K) side chain Salt bridge electrostatic stabiliser -- spectator ICS PubMed:16540464
190 Asn (N) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16540464
197 Asn (N) side chain None -- ISS
198 Asp (D) side chain None -- ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2FUC Human Alpha-Phosphomannomutase 1 With Mg2+ Cofactor Bound Phosphomannomutase 1 10 2.1 Selenomethionine • Magnesium Ion CSA • PDB • PDBSum
2FUE Human Alpha-Phosphomannomutase 1 With D-Mannose 1-Phosphate And Mg2+ Cofactor Bound Phosphomannomutase 1 10 1.75 Selenomethionine
(2 more ⇓) 		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
April 30, 2014, 5:32 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 234 228
EC number assigned by UniProtKB accession ID.