Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.6: HAD, Beta-PGM, Phosphatase Like

  ⌊ FunctionalDomain C1.5.6: HAD, Beta-PGM, Phosphatase Like (ID 117832)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Arabidopsis thaliana Taxon ID: 3702 7268944 PRP URP
Arabidopsis thaliana Taxon ID: 3702 3080391 PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
Bifunctional riboflavin kinase/FMN phosphatase Q84MD8 FHYRK_ARATH (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 282 | Length of Functional Domain: 123

1       10        20        30        40        50        60

MSMSNSLKKLSSCVLIDLDGTLINTDGVVGDILRKYLCKYGKQWDGRESLKIVGKTPVEA
ATTIVEDYELPCKVDEFNSEFYPLFSAQMDKIKSLPGANRLIRHLKCHGVPVALASNSSR
ANIESKISYHEGIENTLPIDPWHIGGPVIKGFGRGSKVLGIPTANLSTKDYADELVEHPS
GVYFGWAGLAKRGVFKMVMSIGWNPYFNNKEKTIEPWLLHDFTEDFYGEELRLIIVGYIR
PEANFSSLESLIAKIHEDREVAEKALDLPSYAKFKGDPYLTK
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
17 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
116 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 1/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
17 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12081483

Catalyzed Reaction

FMN phosphatase

+ +
FMN
17621		 water
15377		 riboflavin
17015		 phosphoric acid
26078

EC: 3.1.3.2 | IntEnz: 3.1.3.2 | Kegg: 3.1.3.2 | BioCyc: 3.1.3.2 | BRENDA: 3.1.3.2

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 7:48 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 136 134
EC number assigned by UniProtKB accession ID.