Q9PPP5 (KITH_UREPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thymidine kinase
EC=2.7.1.21

Gene names

Name:	tdk
Ordered Locus Names:	UU594

Organism

Ureaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]

Taxonomic identifier

273119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Mycoplasmatales › Mycoplasmataceae › Ureaplasma › Ureaplasma parvum › Ureaplasma parvum serovar 3

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + thymidine = ADP + thymidine 5'-phosphate. Ref.3
Subunit structure	Homotetramer. Ref.2 Ref.3
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00124.
Sequence similarities	Belongs to the thymidine kinase family.

Ontologies

Keywords
Biological process	DNA synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP thymidine kinase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 223

223

Thymidine kinase HAMAP-Rule MF_00124

PRO_0000175042

Regions

Nucleotide binding

19 – 26

8

ATP By similarity

Nucleotide binding

96 – 99

4

ATP By similarity

Region

178 – 182

5

Substrate binding HAMAP-Rule MF_00124

Sites

Active site

97

1

Proton acceptor Potential

Metal binding

153

1

Zinc

Metal binding

156

1

Zinc

Metal binding

191

1

Zinc

Metal binding

194

1

Zinc

Binding site

128

1

Substrate; via amide nitrogen

Binding site

187

1

Substrate

Secondary structure

1

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223

Helix Strand Turn

Details...

Beta strand

13 – 18

6

Helix

25 – 38

14

Beta strand

43 – 48

6

Helix

52 – 54

3

Beta strand

69 – 73

5

Helix

75 – 82

8

Beta strand

92 – 95

4

Helix

98 – 100

3

Helix

105 – 114

10

Beta strand

118 – 122

5

Beta strand

130 – 132

3

Helix

136 – 142

7

Beta strand

144 – 148

5

Turn

154 – 156

3

Beta strand

158 – 160

3

Beta strand

162 – 167

6

Turn

184 – 186

3

Beta strand

187 – 190

4

Helix

192 – 194

3

Helix

207 – 215

9

Sequences

	Sequence		Length	Mass (Da)
	Q9PPP5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 27F3061B26979A0B	FASTA	223	25,367
	10 20 30 40 50 60 MAKVNAFSKK IGWIELITGP MFAGKTAELI RRLHRLEYAD VKYLVFKPKI DTRSIRNIQS 70 80 90 100 110 120 RTGTSLPSVE VESAPEILNY IMSNSFNDET KVIGIDEVQF FDDRICEVAN ILAENGFVVI 130 140 150 160 170 180 ISGLDKNFKG EPFGPIAKLF TYADKITKLT AICNECGAEA THSLRKIDGK HADYNDDIVK 190 200 210 220 IGCQEFYSAV CRHHHKVPNR PYLNSNSEEF IKFFKNKKRN KNI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of the mucosal pathogen Ureaplasma urealyticum." Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H. Nature 407:757-762(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700970.
[2]	"Structures of thymidine kinase 1 of human and mycoplasmic origin." Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L., Eriksson S., Munch-Petersen B., Eklund H. Proc. Natl. Acad. Sci. U.S.A. 101:17970-17975(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND THYMIDINE, SUBUNIT.
[3]	"Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme." Kosinska U., Carnrot C., Eriksson S., Wang L., Eklund H. FEBS J. 272:6365-6372(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND THYMIDINE, CATALYTIC ACTIVITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF222894 Genomic DNA. Translation: AAF31008.1.

RefSeq

NP_078433.1. NC_002162.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B8T	X-ray	2.00	A/B/C/D	1-223	[»]
2UZ3	X-ray	2.50	A/B/C/D	1-223	[»]

ProteinModelPortal

Q9PPP5.

SMR

Q9PPP5. Positions 11-217.

ModBase

Search...

Protein-protein interaction databases

STRING

273119.UU594.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAF31008; AAF31008; UU594.

GeneID

876009.

KEGG

uur:UU594.

PATRIC

20534825. VBIUrePar45146_0617.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1435.

HOGENOM

HOG000076390.

KO

K00857.

OMA

KVHAICV.

ProtClustDB

PRK04296.

Enzyme and pathway databases

BioCyc

UPAR273119:GHVP-635-MONOMER.

BRENDA

2.7.1.21. 9209.

Family and domain databases

HAMAP

MF_00124. Thymidine_kinase.

InterPro

IPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[Graphical view]

PANTHER

PTHR11441. PTHR11441. 1 hit.

Pfam

PF00265. TK. 1 hit.
[Graphical view]

PIRSF

PIRSF035805. TK_cell. 1 hit.

SUPFAM

SSF52540. SSF52540. 1 hit.

PROSITE

PS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9PPP5.

ChEMBL

CHEMBL1075130.

EvolutionaryTrace

Q9PPP5.

Entry information

Entry name

KITH_UREPA

Accession

Primary (citable) accession number: Q9PPP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program