Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family galactarolactone cycloisomerase

  ⌊ FunctionalDomain galactarolactone cycloisomerase (ID 291)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:22493433
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Agrobacterium tumefaciens str. C58 Taxon ID: 176299 15891790 NP_357462.1 (RefSeq) URP
Taxon ID: 1183400 499275396 WP_010972789.1 (RefSeq)
Agrobacterium tumefaciens Taxon ID: 358 796557543 KJX87146.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
D-galactarolactone cycloisomerase A9CEQ8 GCI_AGRFC (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 378 | Length of Functional Domain: 378

1       10        20        30        40        50        60

MKITAVRTHLLEHRLDTPFESASMRFDRRAHVLVEIECDDGTVGWGECLGPARPNAAVVQ
AYSGWLIGQDPRQTEKIWAVLYNALRDQGQRGLSLTALSGIDIALWDIKGKHYGASISML
LGGRWRESVRAYATGSFKRDNVDRVSDNASEMAERRAEGFHACKIKIGFGVEEDLRVIAA
VREAIGPDMRLMIDANHGYTVTEAITLGDRAAGFGIDWFEEPVVPEQLDAYARVRAGQPI
PVAGGETWHGRYGMWQALSAGAVDILQPDLCGCGGFSEIQKIATLATLHGVRIVPHVWGT
GVQIAAALQFMAAMTPDPVRVNPIEPIMEFDRTHNPFRQAVLREPLEAVNGVVTIPDGPG
LGIEINRDALTEFRMPDP
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
194 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
220 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
246 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
194 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
220 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
246 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
269 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
296 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
166 Lys (K) side chain Acid/base catalyst proton relay -- reactant ISS PubMed:22493433
194 Asp (D) side chain Metal binding ligand metal ligand -- binding ICS PubMed:26750482
220 Glu (E) side chain Metal binding ligand metal ligand -- binding ICS PubMed:26750482
246 Glu (E) side chain Metal binding ligand metal ligand -- binding ICS PubMed:26750482
269 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ISS PubMed:22493433
296 His (H) side chain General acid--donates proton to beta carbon of substrate as ring opens proton relay -- reactant ISS PubMed:26750482
329 Glu (E) side chain General Acid proton relay -- reactant ISS PubMed:22493433

Catalyzed Reaction

galactarolactone cycloisomerase

D-galactaro-1,4-lactone(1-)
85317		 5-dehydro-4-deoxy-D-glucaric acid
16369

EC: 5.5.1.- | IntEnz: 5.5.1.- | Kegg: 5.5.1.- | BioCyc: 5.5.1.- | BRENDA: 5.5.1.- |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4GGB Crystal Structure Of A Proposed Galactarolactone Cycloisomerase From Agrobacterium Tumefaciens, Target Efi-500704, With Bound Ca, Disordered Loops Putative Uncharacterized Protein 12 2.0 Calcium Ion • Chloride Ion CSA • PDB • PDBSum
4HPN Crystal Structure Of A Proposed Galactarolactone Cycloisomerase From Agrobacterium Tumefaciens, Target Efi-500704, With Bound Ca, Ordered Loops Putative Uncharacterized Protein 12 1.6 Calcium Ion
(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
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
July 9, 2015, 3:08 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update name uncharacterized mandelate racemase subgroup sequence, enolase superfamily galactarolactone cycloisomerase
Sept. 14, 2015, 3:09 a.m. update domain end position 377 378
EC number assigned by UniProtKB accession ID.