Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.3: Phosphomannomutase Like

     ⌊ Family alpha-phosphomannomutase

  ⌊ FunctionalDomain alpha-phosphomannomutase (ID 274518)

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
Homo sapiens Taxon ID: 9606 93279753 PRP URP
Homo sapiens Taxon ID: 9606 93279752 PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
Phosphomannomutase 1 Q92871 5.4.2.8 PMM1_HUMAN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 262 | Length of Functional Domain: 249

1       10        20        30        40        50        60

XAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIA
EQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYXALLR
LPKKRGTFIEFRNGXLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLR
FSRGGXISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSV
VSPQDTVQRCREIFFPETAHEA
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
52 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 8/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
19 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16540464
21 Asp (D) side chain Mg2+ ligand, acid/base metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16540464
62 Gln (Q) side chain Positions acid/base Asp steric role -- spectator ICS PubMed:16540464
188 Ser (S) side chain Binds phosphate substrate binding -- binding ICS PubMed:16540464
198 Lys (K) side chain Salt bridge electrostatic stabiliser -- spectator ICS PubMed:16540464
218 Asn (N) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16540464
225 Asn (N) side chain None -- ISS
226 Asp (D) side chain None -- ISS
Family CAR This EFD conserves 14/14 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
19 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16540464
21 Asp (D) side chain Mg2+ ligand, acid/base metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16540464
28 Arg (R) side chain Binds sbst substrate binding -- binding ICS PubMed:16540464
54 Ser (S) side chain helps position phosphoryl group steric role -- spectator ICS PubMed:16540464
62 Gln (Q) side chain Positions acid/base Asp steric role -- spectator ICS PubMed:16540464
132 Arg (R) side chain Forms positive surface that acts as electrostatic wedge to maintain proper interdomain orientation steric role -- spectator ICS PubMed:16540464
143 Arg (R) side chain Forms positive surface that acts as electrostatic wedge to maintain proper interdomain orientation steric role -- spectator ICS PubMed:16540464
150 Arg (R) side chain Forms positive surface that acts as electrostatic wedge to maintain proper interdomain orientation steric role -- spectator ICS PubMed:16540464
188 Ser (S) side chain Binds phosphate substrate binding -- binding ICS PubMed:16540464
190 Asp (D) side chain Binds sbst substrate binding -- binding ICS PubMed:16540464
198 Lys (K) side chain Salt bridge electrostatic stabiliser -- spectator ICS PubMed:16540464
218 Asn (N) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16540464
225 Asn (N) side chain None -- ISS
226 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, 5:28 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 262 256
update domain start position 12 8
EC number assigned by UniProtKB accession ID.