P65938 (PYRH_STRP1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uridylate kinase
Short name=UK
EC=2.7.4.22

Alternative name(s):
Uridine monophosphate kinase
Short name=UMP kinase
Short name=UMPK

Gene names

Name:	pyrH
Ordered Locus Names:	SPy_0462, M5005_Spy0377/M5005_Spy0378/M5005_Spy0379

Organism

Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]

Taxonomic identifier

301447 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	242 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible phosphorylation of UMP to UDP By similarity. HAMAP MF_01220_B
Catalytic activity	ATP + UMP = ADP + UDP. HAMAP MF_01220_B
Enzyme regulation	Allosterically activated by GTP. Inhibited by UTP By similarity. HAMAP MF_01220_B
Pathway	Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. HAMAP MF_01220_B
Subunit structure	Homohexamer By similarity. HAMAP MF_01220_B
Subcellular location	Cytoplasm By similarity HAMAP MF_01220_B.
Sequence similarities	Belongs to the UMP kinase family.
Sequence caution	The sequence AAZ50995.1 differs from that shown. Reason: Erroneous termination at position 57. Translated as Trp. The sequence AAZ50995.1 differs from that shown. Reason: Frameshift at positions 65 and 115. The sequence AAZ50996.1 differs from that shown. Reason: Frameshift at positions 65 and 115. The sequence AAZ50997.1 differs from that shown. Reason: Frameshift at positions 65 and 115.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	cellular amino acid biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process 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: UniProtKB-KW UMP 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 – 242

242

Uridylate kinase HAMAP MF_01220_B

PRO_0000143894

Regions

Nucleotide binding

11 – 14

4

ATP By similarity

Nucleotide binding

134 – 141

8

UMP By similarity

Region

19 – 24

6

Involved in allosteric activation by GTP Potential

Sites

Binding site

53

1

UMP; via amide nitrogen By similarity

Binding site

54

1

ATP; via amide nitrogen By similarity

Binding site

58

1

ATP By similarity

Binding site

73

1

UMP By similarity

Binding site

162

1

ATP By similarity

Binding site

168

1

ATP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

171

1

ATP By similarity

Experimental info

Sequence conflict

58

1

R → C Ref.2

Secondary structure

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242

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

14 – 17

4

Beta strand

20 – 24

5

Helix

27 – 41

15

Turn

42 – 44

3

Beta strand

46 – 51

6

Turn

54 – 56

3

Helix

59 – 65

7

Helix

69 – 92

24

Turn

93 – 95

3

Beta strand

98 – 104

7

Turn

107 – 109

3

Beta strand

110 – 112

3

Helix

115 – 123

9

Beta strand

127 – 132

6

Helix

141 – 151

11

Beta strand

155 – 163

9

Beta strand

168 – 170

3

Turn

172 – 174

3

Beta strand

182 – 185

4

Helix

186 – 190

5

Turn

191 – 193

3

Helix

199 – 207

9

Beta strand

211 – 216

6

Helix

222 – 227

6

Beta strand

233 – 237

5

Sequences

	Sequence		Length	Mass (Da)
	P65938 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: B4517145A5160433	FASTA	242	25,896
	10 20 30 40 50 60 MEPKYQRILI KLSGEALAGE KGVGIDIPTV QAIAKEIAEV HVSGVQIALV IGGGNLWRGE 70 80 90 100 110 120 PAADAGMDRV QADYTGMLGT VMNALVMADS LQHYGVDTRV QTAIPMQNVA EPYIRGRALR 130 140 150 160 170 180 HLEKNRIVVF GAGIGSPYFS TDTTAALRAA EIEADAILMA KNGVDGVYNA DPKKDANAVK 190 200 210 220 230 240 FDELTHGEVI KRGLKIMDAT ASTLSMDNDI DLVVFNMNEA GNIQRVVFGE HIGTTVSNKV CD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E. Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed: 11296296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1.
[2]	"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed: 16088826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.
[3]	"Crystal structure of a putative uridylate kinase (UMP-kinase) from Streptococcus pyogenes." New York structural genomics research consortium (NYSGRC) Submitted (APR-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE004092 Genomic DNA. Translation: AAK33476.1.
CP000017 Genomic DNA. Translation: AAZ50995.1. Sequence problems.
CP000017 Genomic DNA. Translation: AAZ50996.1. Sequence problems.
CP000017 Genomic DNA. Translation: AAZ50997.1. Sequence problems.

RefSeq

NP_268755.1. NC_002737.1.
YP_281740.1. NC_007297.1.
YP_281741.1. NC_007297.1.
YP_281742.1. NC_007297.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z9D	X-ray	2.80	A/B/C	2-242	[»]

ProteinModelPortal

P65938.

SMR

P65938. Positions 2-239.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTRT00000001193; EBSTRP00000001193; EBSTRG00000001193.
EBSTRT00000027710; EBSTRP00000026728; EBSTRG00000027710.
EBSTRT00000027792; EBSTRP00000026810; EBSTRG00000027792.
EBSTRT00000029159; EBSTRP00000028177; EBSTRG00000029159.

GeneID

3572549.
3572550.
3572551.
900704.

GenomeReviews

Gene locus SPy_0462 in contig AE004092_GR.

KEGG

spy:SPy_0462.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000028290.

HOGENOM

HBG497552.

OMA

RHMEKGR.

Enzyme and pathway databases

BioCyc

SPYO160490:SPY0462-MONOMER.
SPYO293653:M5005_SPY0377-MONOMER.
SPYO293653:M5005_SPY0378-MONOMER.
SPYO293653:M5005_SPY0379-MONOMER.

Family and domain databases

HAMAP

MF_01220_B. PyrH_B.
[Tree]

InterPro

IPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

KO

K09903.

PANTHER

PTHR26059. PTHR26059. 1 hit.

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF005650. Uridylate_kin. 1 hit.

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR02075. PyrH_bact. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PYRH_STRP1

Accession

Primary (citable) accession number: P65938
Secondary accession number(s): P59007 , Q490H1, Q490H2, Q490H3, Q9A151

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program