Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mannonate dehydratase

  ⌊ FunctionalDomain uncharacterized mannonate dehydratase subgroup sequence, enolase superfamily (ID 1396562)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Novosphingobium aromaticivorans DSM 12444 Taxon ID: 279238 609412269 URP
Novosphingobium aromaticivorans DSM 12444 Taxon ID: 279238 609412268 URP
Novosphingobium aromaticivorans DSM 12444 Taxon ID: 279238 609412267 URP
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Uniprot

Protein NameAccessionEC Number Identifier
D-mannonate dehydratase A4XF23 4.2.1.8 MAND_NOVAD (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 418 | Length of Functional Domain: 403

1       10        20        30        40        50        60

HHHHHHSSGLVPRGSHMKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVV
AYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMP
LYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRG
KLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLG
KMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRA
TVVGAGGLTHLRRIADLASLYQVRTGCHGPTDLSPVTMGCALHFDTWVPNFGIQEYMRHT
EETDAVFPHDYWFEKGELFVGETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
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 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
226 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
252 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
278 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 8/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
163 Arg (R) side chain controls pKa of catalytic Tyr perturbates pKa -- spectator ICS PubMed:17944491
175 Tyr (Y) side chain abstracts proton from C2 of substrate; may facilitate departure of 3-OH leaving group proton relay -- reactant ICS PubMed:17944491
226 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17944491
228 His (H) side chain may facilitate departure of 3-OH leaving group increase electrophilicity -- spectator ICS PubMed:17944491
252 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17944491
278 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17944491
299 Arg (R) side chain electrophilic catalyst, stabilizes enolate anion intermediate covalent catalysis -- reactant,
electrostatic stabiliser -- spectator 		ICS PubMed:17944491
355 Glu (E) side chain electrophilic catalyst, stabilizes enolate anion intermediate covalent catalysis -- reactant,
electrostatic stabiliser -- spectator 		ICS PubMed:17944491

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4K1W Crystal Structure Of The A314P Mutant Of Mannonate Dehydratase From Novosphingobium Aromaticivorans Complexed With Mg And D-Mannonate Mandelate Racemase/Muconate Lactonizing Enzyme, N-Terminaldomain Protein 7 1.65 Yes Magnesium Ion
(5 more ⇓) 		CSA • PDB • PDBSum
2QJN Crystal Structure Of D-Mannonate Dehydratase From Novosphingobium Aromaticivorans Complexed With Mg And 2-Keto-3-Deoxy-D-Gluconate Mandelate Racemase/Muconate Lactonizing Enzyme 7 2.0 Magnesium Ion • 2-Keto-3-Deoxygluconate CSA • PDB • PDBSum
2QJJ Crystal Structure Of D-Mannonate Dehydratase From Novosphingobium Aromaticivorans Mandelate Racemase/Muconate Lactonizing Enzyme 7 1.8 Magnesium Ion CSA • PDB • PDBSum
2QJM Crystal Structure Of The K271E Mutant Of Mannonate Dehydratase From Novosphingobium Aromaticivorans Complexed With Mg And D-Mannonate Mandelate Racemase/Muconate Lactonizing Enzyme 7 2.2 Yes Magnesium Ion • D-Mannonic Acid CSA • PDB • PDBSum
4K8G Crystal Structure Of D-Mannonate Dehydratase From Novosphingobium Aromaticivorans Mutant (V161A, R163A, K165G, L166A, Y167G, Y168A, E169G) Mandelate Racemase/Muconate Lactonizing Enzyme, N-Terminaldomain Protein 4 1.25 Yes Glycerol • 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, 3:02 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
June 8, 2015, 3:28 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
remove family assignment evidence code IEA -
remove family mannonate dehydratase -
update name mannonate dehydratase uncharacterized mannonate dehydratase subgroup sequence, enolase superfamily
July 9, 2015, 3:27 a.m. update domain start position 17 16
EC number assigned by UniProtKB accession ID.