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O04905 (KCY_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UMP-CMP kinase
EC=2.7.4.14
Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK
Gene names
Name:PYR6
Ordered Locus Names:At5g26667
ORF Names:T7I7.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Does not act on dCMP and dUMP. HAMAP-Rule MF_03172

Catalytic activity

ATP + (d)CMP = ADP + (d)CDP. Ref.1

ATP + UMP = ADP + UDP. Ref.1

Cofactor

Binds 1 magnesium ion per monomer By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_03172

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=29.3 µM for ATP (with UMP as cosubstrate) Ref.1

KM=291.7 µM for ATP (with CMP as cosubstrate)

KM=152.9 µM for UMP

KM=266.4 µM for CMP

pH dependence:

Optimum pH is 6.5.

Mass spectrometry

Molecular mass is 22405±185 Da from positions 1 - 202. Determined by MALDI. Ref.1

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O04905-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202UMP-CMP kinase HAMAP-Rule MF_03172
PRO_0000158945

Regions

Nucleotide binding24 – 296ATP By similarity
Nucleotide binding71 – 733NMP By similarity
Nucleotide binding98 – 1014NMP By similarity
Region44 – 7330NMPbind By similarity
Region136 – 1449LID By similarity

Sites

Binding site501NMP By similarity
Binding site1051CMP By similarity
Binding site1371ATP By similarity
Binding site1411NMP By similarity
Binding site1521NMP By similarity
Binding site1801ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 41AD0CFACD816315

FASTA20222,482
        10         20         30         40         50         60 
MGSVDAANGS GKKPTVIFVL GGPGSGKGTQ CAYIVEHYGY THLSAGDLLR AEIKSGSENG 

        70         80         90        100        110        120 
TMIQNMIKEG KIVPSEVTIK LLQKAIQENG NDKFLIDGFP RNEENRAAFE KVTEIEPKFV 

       130        140        150        160        170        180 
LFFDCPEEEM EKRLLGRNQG REDDNIETIR KRFKVFLESS LPVIHYYEAK GKVRKINAAK 

       190        200 
PIEAVFEEVK AIFSPEAEKV EA

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase."
Zhou L., Lacroute F., Thornburg R.
Plant Physiol. 117:245-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-15, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION MECHANISM.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF000147 mRNA. Translation: AAB71135.1.
AC137518 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93559.1.
CP002688 Genomic DNA. Translation: AED93560.1.
IPIIPI00525198.
RefSeqNP_001031942.1. NM_001036865.1.
NP_850868.1. NM_180537.2.
UniGeneAt.10397.

3D structure databases

ProteinModelPortalO04905.
SMRO04905. Positions 13-193.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT5G26667.1-P.

Proteomic databases

PaxDbO04905.
PRIDEO04905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G26667.2; AT5G26667.2; AT5G26667.
AT5G26667.3; AT5G26667.3; AT5G26667.
GeneID832710.
KEGGath:AT5G26667.

Organism-specific databases

TAIRAt5g26667.

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238771.
InParanoidO04905.
KOK13800.
PhylomeDBO04905.
ProtClustDBCLSN2918278.

Enzyme and pathway databases

BioCycARA:AT5G26667-MONOMER.
MetaCyc:AT5G26667-MONOMER.

Gene expression databases

GenevestigatorO04905.

Family and domain databases

HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProIPR000850. Adenylate_kin.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF00406. ADK. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
TIGRFAMsTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKCY_ARATH
AccessionPrimary (citable) accession number: O04905
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents