Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.4: Enolase-phosphatase Like

     ⌊ Family enolase-phosphatase

  ⌊ FunctionalDomain enolase-phosphatase (ID 1447)

Superfamily Assignment Evidence Code(s) FSM PubMed:9649311
Family Assignment Evidence Code CFM PubMed:8227040
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 543 636832817 WP_024358822.1 (RefSeq)
n/a 14107742 AAE56596.1 (Genbank)
Klebsiella oxytoca Taxon ID: 571 401712 AAC43183.1 (Genbank) URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_01681} Q48389 MTNC_KLEOX (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 229 | Length of Functional Domain: 227

1       10        20        30        40        50        60

MIRAIVTDIEGTTSDIRFVHNVLFPYARERLAGFVTAQQFVEPVKTILDNLREEIAQPAA
GAEELIATLFAFMDEDRKSTALKALQGIIWRDGYVHGDFTGHLYPDVLPALEKWKSQGID
LYVYSSGSVAAQKLLFGYSDEGDITHLFNGYFDTLVGAKREAQSYRNIAEQLGQPPAAIL
FLSDIHQELDAAEEAGFRTLQLVRGDRDPASHHPQVQRFDDIHPEQIPA
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 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
125 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15843022
126 Ser (S) side chain binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:15843022
159 Lys (K) side chain Forms salt bridge with nucleophilic Asp; binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack -- ICS PubMed:15843022
184 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15843022
188 Glu (E) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15843022
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15843022
12 Thr (T) side chain None -- ISS PubMed:9649311
126 Ser (S) side chain binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:15843022
159 Lys (K) side chain Forms salt bridge with nucleophilic Asp; binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack -- ICS PubMed:15843022
184 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15843022
188 Glu (E) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15843022

Catalyzed Reaction

acireductone synthase

+ +
5-(methylsulfanyl)-2,3-dioxopentyl phosphate(2-)
58828		 water
15377		 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
49252		 hydrogenphosphate
43474

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

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:22 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.