Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family 3,6-anhydro-alpha-L-galactonate cycloisomerase

  ⌊ FunctionalDomain 3,6-anhydro-alpha-L-galactonate cycloisomerase (ID 300020)

Superfamily Assignment Evidence Code(s) IES PubMed:25156229
Family Assignment Evidence Code IES PubMed:25156229
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Vibrio sp. EJY3 Taxon ID: 1116375 503998237 WP_014232231.1 (RefSeq) URP
Vibrio sp. EJY3 Taxon ID: 1116375 369841212 AEX22356.1 (Genbank) URP
Vibrio sp. EJY3 Taxon ID: 1116375 765680539 URP

Uniprot

Protein NameAccessionEC Number Identifier
3,6-anhydro-alpha-L-galactonate cycloisomerase {ECO:0000305} H2IFX0 ACI_VIBSJ (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 362 | Length of Functional Domain: 362

1       10        20        30        40        50        60

MKTTIKDIKTRLFKIPLKEILSDAKHGDHDHFELITTTVTLEDGSQGTGYTYTGGKGGYS
IKAMLEYDIQPALIGKDATQIEEIYDFMEWHIHYVGRGGISTFAMSAVDIALWDLKGKRE
GLPLWKMAGGKNNTCKAYCGGIDLQFPLEKLLNNICGYLESGFNAVKIKIGRENMQEDID
RIKAVRELIGPDITFMIDANYSLTVEQAIKLSKAVEQYDITWFEEPTLPDDYKGFAEIAD
NTAIPLAMGENLHTIHEFGYAMDQAKLGYCQPDASNCGGITGWLKAADLITEHNIPVCTH
GMQELHVSLVSAFDTGWLEVHSFPIDEYTKRPLVVENFRAVASNEPGIGVEFDWDKIAQY
EV
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
198 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
224 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
250 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
198 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
224 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
250 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
273 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
300 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
169 Lys (K) side chain None -- ISS
198 Asp (D) side chain metal binding ligand metal ligand -- binding ISS
224 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
250 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
273 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS
300 His (H) side chain None -- ISS
319 Glu (E) side chain None -- ISS

Catalyzed Reaction

3,6-anhydro-alpha-L-galactonate cycloisomerase

3,6-anhydro-L-galactonate
83435		 2-keto-3-deoxy-L-galactonate
75545

EC: 5.5.1.25 | IntEnz: 5.5.1.25 | Kegg: 5.5.1.25 | BioCyc: 5.5.1.25 | BRENDA: 5.5.1.25

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 2:46 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
July 9, 2015, 3:16 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update name uncharacterized mandelate racemase subgroup sequence 3,6-anhydro-alpha-L-galactonate cycloisomerase
update domain start position 2 1
update superfamily assignment evidence code IEA IES
EC number assigned by UniProtKB accession ID.