2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase - Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

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P43777 (HPPK_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. 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:	HI_0064

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
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.
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 Reference proteome
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 160

160

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

PRO_0000168250

Secondary structure

160

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P43777 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 136CD15F8844FDDD
Show »

FASTA

160

18,299

        10         20         30         40         50         60 
MITAYIALGS NLNTPVEQLH AALKAISQLS NTHLVTTSSF YKSKPLGPQD QPDYVNAVAK 

        70         80         90        100        110        120 
IETELSPLKL LDELQRIENE QGRVRLRRWG ERTLDLDILL YGNEIIQNER LTIPHYDMHN 

       130        140        150        160 
REFVIVPLFE IASDLVLPNS QIITELVKQF ADHKMIKLNP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae." Hennig M., Dale G.E., D'Arcy A., Danel F., Fischer S., Gray C.P., Jolidon S., Mueller F., Page M.G.P., Pattison P., Oefner C. J. Mol. Biol. 287:211-219(1999) [PubMed: 10080886] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42023 Genomic DNA. Translation: AAC21742.1.

RefSeq

NP_438237.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CBK	X-ray	2.02	A/B	1-160	[»]

ProteinModelPortal

P43777.

SMR

P43777. Positions 1-160.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

950962.

GenomeReviews

Gene locus HI_0064 in contig L42023_GR.

KEGG

hin:HI0064.

NMPDR

fig|71421.1.peg.63.

PATRIC

20188583. VBIHaeInf48452_0065.

TIGR

HI_0064.

Phylogenomic databases

HOGENOM

HBG662565.

OMA

ETDPVGY.

PhylomeDB

P43777.

ProtClustDB

CLSK870279.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0064-MONOMER.

Family and domain databases

InterPro

IPR000550. Hppk.
[Graphical view]

Gene3D

G3DSA:3.30.70.560. Hppk. 1 hit.

K00950.

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...

Entry information

Entry name

HPPK_HAEIN

Accession

Primary (citable) accession number: P43777

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program