Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup glucarate dehydratase

     ⌊ Family glucarate dehydratase

  ⌊ FunctionalDomain glucarate dehydratase (ID 4920)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 469 491069052 WP_004930680.1 (RefSeq)
Acinetobacter baylyi DSM 14961 = CIP 107474 Taxon ID: 1120924 480011604 ENV53022.1 (Genbank) URP
Acinetobacter sp. ADP1 Taxon ID: 62977 81393997 URP
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Uniprot

Protein NameAccessionEC Number Identifier
Glucarate dehydratase Q6FFQ2 4.2.1.40 GUDD_ACIAD (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 444 | Length of Functional Domain: 444

1       10        20        30        40        50        60

MAASTPIIQSVRAIPVAGHDSMLLNLSGAHAPYFTRNLLVIEDNSGNIGVGEIPGGEKIL
ATLNDAKSLILGQPIGEYKNLLKKIHQTFADRDSGGRGNQTFDLRTTVHVVTAYESALLD
LLGKHLNVNVASLLGDGQQRDEVEVLGYLFFIGDRKQTSLDYATSTHLNHDWYQVRHEKA
LTPEAIQRLAEASYDRYGFKDFKLKGGVLHGEQEAEAVTAIARRFPDARVTLDPNGAWYL
DEAIGLGKHLKGVLAYAEDPCGAEQGYSSREIMAEFKRATGLPTATNMIATDWREMSHSI
QLQAVDIPLADPHFWTLEGSVRVSQLCNMYNLTWGSHSNNHFDVSLAMFTHVAAAAVGNV
TAIDTHWIWQEGTDHLTKQPLEIKGGKIQVPSVPGLGVELDWDNINRAHELYKAKGLGAR
NDADAMQFMVPNWKFDHKKPCLVR
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
233 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
258 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
287 Asn (N) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
205 Lys (K) side chain abstracts alpha proton from l-stereochemistry substrates proton relay -- reactant ISS PubMed:10769114
233 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
258 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
287 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
311 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS PubMed:10769114
337 His (H) side chain abstracts alpha proton from d-stereochemistry substates proton relay -- reactant ISS PubMed:10769114
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
205 Lys (K) side chain abstracts alpha proton from l-idarate proton relay -- reactant IDA PubMed:11513584
233 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
258 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
287 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
311 Asp (D) side chain controls pKa of H385 perturbates pKa -- spectator ICS PubMed:10769114
337 His (H) side chain abstracts alpha proton from d-glucarate proton relay -- reactant IDA PubMed:11513584
339 Asn (N) side chain general acid (facilitates departure of 4-OH and stereospecific tautomerization) OR positions H339 to act as general acid proton relay -- reactant IDA PubMed:11513584

Catalyzed Reaction

glucarate dehydratase

+
D-glucarate(2-)
30612		 5-dehydro-4-deoxy-D-glucarate(2-)
42819		 water
15377

EC: 4.2.1.40 | IntEnz: 4.2.1.40 | Kegg: 4.2.1.40 | BioCyc: 4.2.1.40 | BRENDA: 4.2.1.40

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.