2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

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P26281 (HPPK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
EC=2.7.6.3

Alternative name(s):
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
Short name=PPPK
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
Short name=HPPK

Gene names

Name:	folK
Ordered Locus Names:	b0142, JW0138

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Subunit structure	Monomer.
Miscellaneous	This enzyme is heat stable.
Sequence similarities	Belongs to the HPPK family.

Ontologies

Keywords
Biological process	Folate biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Inferred from direct assay Ref.5. Source: EcoCyc ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from direct assay PubMed 10825540. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.5

Chain

2 – 159

158

2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

PRO_0000168249

Secondary structure

159

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P26281 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 67301CD634D0A174
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FASTA

159

18,079

        10         20         30         40         50         60 
MTVAYIAIGS NLASPLEQVN AALKALGDIP ESHILTVSSF YRTPPLGPQD QPDYLNAAVA 

        70         80         90        100        110        120 
LETSLAPEEL LNHTQRIELQ QGRVRKAERW GPRTLDLDIM LFGNEVINTE RLTVPHYDMK 

       130        140        150 
NRGFMLWPLF EIAPELVFPD GEMLRQILHT RAFDKLNKW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase." Talarico T.L., Ray P.H., Dev I.K., Merrill B.M., Dallas W.S. J. Bacteriol. 174:5971-5977(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100." Talarico T.L., Dev I.K., Dallas W.S., Ferone R., Ray P.H. J. Bacteriol. 173:7029-7032(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-29.
[6]	"Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control." Liu J., Parkinson J.S. J. Bacteriol. 171:1254-1261(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[7]	"Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents." Xiao B., Shi G., Chen X., Yan H., Ji X. Structure 7:489-496(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[8]	"2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue." Stammers D.K., Achari A., Somers D.O., Bryant P.K., Rosemond J., Scott D.L., Champness J.N. FEBS Lett. 456:49-53(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06495 Genomic DNA. Translation: AAB53446.1.
M20574 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73253.1.
AP009048 Genomic DNA. Translation: BAB96719.1.

PIR

A43325.

RefSeq

NP_414684.1. NC_000913.2.
YP_488445.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DY3	X-ray	2.00	A	2-159	[»]
1EQ0	NMR	-	A	2-158	[»]
1EQM	X-ray	1.50	A	2-158	[»]
1EX8	X-ray	1.85	A	2-158	[»]
1F9H	X-ray	1.50	A	2-158	[»]
1G4C	X-ray	1.65	A/B	2-158	[»]
1HKA	X-ray	1.50	A	2-159	[»]
1HQ2	X-ray	1.25	A	2-158	[»]
1IM6	X-ray	1.74	A	2-158	[»]
1KBR	X-ray	1.55	A	2-158	[»]
1Q0N	X-ray	1.25	A	2-158	[»]
1RAO	X-ray	1.56	A	2-158	[»]
1RB0	X-ray	1.35	A	2-158	[»]
1RTZ	X-ray	1.33	A	2-158	[»]
1RU1	X-ray	1.40	A/B	2-158	[»]
1RU2	X-ray	1.48	A	2-158	[»]
1TMJ	X-ray	1.45	A	2-158	[»]
1TMM	X-ray	1.25	A/B	2-158	[»]
2F63	NMR	-	A	2-158	[»]
2F65	NMR	-	A	2-158	[»]
3HCX	X-ray	1.75	A	2-159	[»]
3HD1	X-ray	1.30	A	2-159	[»]
3HD2	X-ray	1.10	A	2-159	[»]
3HSD	X-ray	1.65	A/B	2-159	[»]
3HSG	X-ray	1.14	A	2-159	[»]
3HSJ	X-ray	1.18	A	2-159	[»]
3HSZ	X-ray	1.40	A	2-159	[»]
3HT0	X-ray	1.40	A	2-159	[»]
3ILI	X-ray	1.45	A	2-159	[»]
3ILJ	X-ray	1.65	A	2-159	[»]
3ILL	X-ray	1.73	A	2-159	[»]
3ILO	X-ray	1.10	A	2-159	[»]
3IP0	X-ray	0.89	A	2-159	[»]
3KUE	X-ray	1.54	A	2-159	[»]
3KUG	X-ray	2.00	A	2-159	[»]
3KUH	X-ray	1.35	A	2-159	[»]
3UD5	X-ray	2.00	A	2-159	[»]
3UDE	X-ray	1.88	A	2-159	[»]
3UDV	X-ray	1.88	A	2-159	[»]
4F7V	X-ray	1.73	A	2-159	[»]

ProteinModelPortal

P26281.

SMR

P26281. Positions 2-159.

ModBase

Search...

Protein-protein interaction databases

IntAct

P26281. 2 interactions.

STRING

511145.b0142.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73253; AAC73253; b0142.
BAB96719; BAB96719; BAB96719.

GeneID

12934036.
948792.

KEGG

ecj:Y75_p0139.
eco:b0142.

PATRIC

32115391. VBIEscCol129921_0147.

Organism-specific databases

EchoBASE

EB1348.

EcoGene

EG11374. folK.

Phylogenomic databases

eggNOG

COG0801.

HOGENOM

HOG000217741.

K00950.

OMA

DQDWFLN.

ProtClustDB

PRK10239.

Enzyme and pathway databases

BioCyc

EcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
ECOL316407:JW0138-MONOMER.
MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.

SABIO-RK

P26281.

UniPathway

UPA00077; UER00155.

Gene expression databases

Genevestigator

P26281.

Family and domain databases

Gene3D

3.30.70.560. 1 hit.

InterPro

IPR000550. Hppk.
[Graphical view]

Pfam

PF01288. HPPK. 1 hit.
[Graphical view]

SUPFAM

SSF55083. Hppk. 1 hit.

TIGRFAMs

TIGR01498. folK. 1 hit.

PROSITE

PS00794. HPPK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P26281.

Entry information

Entry name

HPPK_ECOLI

Accession

Primary (citable) accession number: P26281

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents