P82197 (PDXK_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyridoxal kinase
EC=2.7.1.35

Alternative name(s):
Pyridoxine kinase

Gene names

Name:	PDXK
Synonyms:	PKH

Organism

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for synthesis of pyridoxal-5-phosphate from vitamin B6.
Catalytic activity	ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Cofactor	Divalent cations. Zinc is more efficient than magnesium. Ref.4
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the pyridoxine kinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	pyridoxal 5'-phosphate salvage Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 312

312

Pyridoxal kinase

PRO_0000213339

Regions

Nucleotide binding

186 – 187

2

ATP

Nucleotide binding

223 – 234

12

ATP

Sites

Binding site

12

1

Substrate

Binding site

47

1

Substrate

Binding site

127

1

Substrate

Binding site

235

1

Substrate

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Modified residue

59

1

Phosphoserine By similarity

Modified residue

84

1

Phosphotyrosine By similarity

Modified residue

164

1

Phosphoserine By similarity

Modified residue

196

1

Phosphoserine By similarity

Modified residue

204

1

Phosphoserine By similarity

Modified residue

213

1

Phosphoserine By similarity

Modified residue

259

1

Phosphothreonine By similarity

Modified residue

285

1

Phosphoserine By similarity

Experimental info

Sequence conflict

16 – 47

32

RGYVG…FSNHT → MCFGGTAESLCPGDLMQHRG LTWSALPPTPPP Ref.2

Sequence conflict

61 – 62

2

EL → DV in AAD34353. Ref.2

Sequence conflict

189

1

N → D in AAD34353. Ref.2

Secondary structure

1

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312

Helix Strand Turn

Details...

Beta strand

6 – 17

12

Helix

21 – 30

10

Beta strand

34 – 45

12

Beta strand

54 – 56

3

Helix

59 – 71

13

Beta strand

78 – 82

5

Helix

88 – 104

17

Beta strand

109 – 112

4

Beta strand

122 – 124

3

Helix

130 – 132

3

Helix

133 – 138

6

Helix

141 – 143

3

Beta strand

145 – 147

3

Helix

151 – 158

8

Helix

165 – 178

14

Beta strand

181 – 185

5

Beta strand

198 – 207

10

Beta strand

215 – 224

10

Helix

233 – 247

15

Helix

252 – 277

26

Turn

286 – 289

4

Helix

294 – 296

3

Helix

297 – 301

5

Sequences

	Sequence		Length	Mass (Da)
	P82197 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: C5F286DBCF51CA6A	FASTA	312	34,819
	10 20 30 40 50 60 MEEECRVLSI QSHVVRGYVG NRAATFPLQV LGFEVDAVNS VQFSNHTGYS HWKGQVLNSD 70 80 90 100 110 120 ELQELYDGLK LNHVNQYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVMGDQR 130 140 150 160 170 180 NGEGAMYVPD DLLPVYREKV VPVADIITPN QFEAELLTGR KIHSQEEALE VMDMLHSMGP 190 200 210 220 230 240 DTVVITSSNL LSPRGSDYLM ALGSQRTRAP DGSVVTQRIR MEMHKVDAVF VGTGDLFAAM 250 260 270 280 290 300 LLAWTHKHPN NLKVACEKTV SAMHHVLQRT IKCAKAKSGE GVKPSPAQLE LRMVQSKKDI 310 ESPEIVVQAT VL

References

[1]	"Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues." Maras B., Valiante S., Orru S., Simmaco M., Barra D., Churchich J.E. J. Protein Chem. 18:259-268(1999) [PubMed: 10395444] [Abstract] Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE OF 113-259. Tissue: Brain.
[2]	Kwon O.-S., Lee H.-S. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-312. Tissue: Liver.
[3]	"Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain." Li M.-H., Kwok F., An X.-M., Chang W.-R., Lau C.-K., Zhang J.-P., Liu S.-Q., Leung Y.-C., Jiang T., Liang D.-C. Acta Crystallogr. D 58:1479-1481(2002) [PubMed: 12198308] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP.
[4]	"Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily." Li M.-H., Kwok F., Chang W.-R., Lau C.-K., Zhang J.-P., Lo S.C.L., Jiang T., Liang D.-C. J. Biol. Chem. 277:46385-46390(2002) [PubMed: 12235162] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ADP AND COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF125374 mRNA. Translation: AAD34353.1.

RefSeq

NP_001009220.1. NM_001009220.1.

UniGene

Oar.696.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LHP	X-ray	2.10	A/B	1-312	[»]
1LHR	X-ray	2.60	A/B	1-312	[»]
1RFT	X-ray	2.80	A	1-312	[»]
1RFU	X-ray	2.80	A/B/C/D/E/F/G/H	1-312	[»]
1RFV	X-ray	2.80	A/B	1-312	[»]
1YGJ	X-ray	2.70	A	1-312	[»]
1YGK	X-ray	2.60	A	1-312	[»]
1YHJ	X-ray	2.80	A	1-312	[»]

ProteinModelPortal

P82197.

SMR

P82197. Positions 1-312.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

443049.

Organism-specific databases

CTD

8566.

Phylogenomic databases

HOVERGEN

HBG000732.

Family and domain databases

InterPro

IPR011611. Carb/pur_kinase.
IPR004625. PyrdxlP_synth_PyrdxlKinase.
[Graphical view]

PANTHER

PTHR10534. PTHR10534. 1 hit.

Pfam

PF00294. PfkB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00687. Pyridox_kin. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PDXK_SHEEP

Accession

Primary (citable) accession number: P82197
Secondary accession number(s): Q9XSD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	October 19, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program