Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.5: Heptose Bisphosphate Phosphatase Like

     ⌊ Family histidinol-phosphatase

  ⌊ FunctionalDomain histidinol-phosphatase (ID 2264)

Superfamily Assignment Evidence Code(s) FSM PubMed:7966317
Family Assignment Evidence Code CFM PubMed:3007936
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 90111373 NP_416526.4 (RefSeq) URP
Taxon ID: 543 446002250 WP_000080105.1 (RefSeq)
Escherichia coli Taxon ID: 562 857141086 AKO57553.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022} P06987 HIS7_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 355 | Length of Functional Domain: 195

1       10        20        30        40        50        60

MSQKYLFIDRDGTLISEPPSDFQVDRFDKLAFEPGVIPELLKLQKAGYKLVMITNQDGLG
TQSFPQADFDGPHNLMMQIFTSQGVQFDEVLICPHLPADECDCRKPKVKLVERYLAEQAM
DRANSYVIGDRATDIQLAENMGITGLRYDRETLNWPMIGEQLTRRDRYAHVVRNTKETQI
DVQVWLDREGGSKINTGVGFFDHMLDQIATHGGFRMEINVKGDLYIDDHHTVEDTGLALG
EALKIALGDKRGICRFGFVLPMDECLARCALDISGRPHLEYKAEFTYQRVGDLSTEMIEH
FFRSLSYTMGVTLHLKTKGKNDHHRVESLFKAFGRTLRQAIRVEGDTLPSSKGVL
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
54 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:20050614
11 Asp (D) side chain general acid, general base; Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20050614
17 Glu (E) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:20050614
54 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
105 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
130 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:20050614
Family CAR This EFD conserves 4/4 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant ISS PubMed:7966317
11 Asp (D) side chain None -- ISS PubMed:7966317
105 Lys (K) side chain None -- ISS PubMed:7966317
130 Asp (D) side chain None -- ISS PubMed:7966317

Catalyzed Reaction

histidinol-phosphatase

+ +
L-histidinol phosphate(1-)
57980		 water
15377		 L-histidinol(1+)
57699		 hydrogenphosphate
43474

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

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.