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 105787)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella flexneri 2a str. 301 Taxon ID: 198214 24115109 NP_709619.1 (RefSeq)
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16131664 NP_418257.1 (RefSeq) URP
Taxon ID: 543 447136328 WP_001213584.1 (RefSeq)
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Uniprot

Protein NameAccessionEC Number Identifier
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB {ECO:0000303|PubMed:24123841} P0ADP0 YIGB_ECOLI (Swiss-Prot)
Flavin mononucleotide phosphatase YigB P0ADP1 3.1.3.- YIGB_SHIFL (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 238 | Length of Functional Domain: 231

1       10        20        30        40        50        60

MRFYRPLGRISALTFDLDDTLYDNRPVILRTEREALTFVQNYHPALRSFQNEDLQRLRQA
VREAEPEIYHDVTRWRFRSIEQAMLDAGLSAEEASAGAHAAMINFAKWRSRIDVPQQTHD
TLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYFLAAEKLNVPI
GEILHVGDDLTTDVGGAIRSGMQACWIRPENGDLMQTWDSRLLPHLEISRLASLTSLI
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 1/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
135 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
16 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
163 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483

Catalyzed Reaction

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

+ +
5-amino-6-(5-phospho-D-ribitylamino)uracil
18247		 water
15377		 5-amino-6-(D-ribitylamino)uracil
15934		 phosphoric acid
26078

EC: 3.1.3.- | IntEnz: 3.1.3.- | Kegg: 3.1.3.- | BioCyc: 3.1.3.- | BRENDA: 3.1.3.- |

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 4:26 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.