KCY_SULAC
ID KCY_SULAC Reviewed; 182 AA.
AC O05982; Q4JB67;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytidylate kinase;
DE Short=CK;
DE EC=2.7.4.25;
DE AltName: Full=Cytidine monophosphate kinase;
DE Short=CMP kinase;
GN Name=cmk; Synonyms=cdk; OrderedLocusNames=Saci_0570;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA Kath T., Schaefer G., Moll R.;
RT "The downstream region of the Sulfolobus adk gene comprises the r134- and
RT the cytidylate kinase gene.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Y13049; CAA73486.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79962.1; -; Genomic_DNA.
DR RefSeq; WP_011277464.1; NC_007181.1.
DR AlphaFoldDB; O05982; -.
DR SMR; O05982; -.
DR STRING; 330779.Saci_0570; -.
DR PRIDE; O05982; -.
DR EnsemblBacteria; AAY79962; AAY79962; Saci_0570.
DR GeneID; 3473208; -.
DR KEGG; sai:Saci_0570; -.
DR PATRIC; fig|330779.12.peg.549; -.
DR eggNOG; arCOG01037; Archaea.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; FIFRDMA; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02020; CMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR InterPro; IPR011892; Cyt_kin_arch.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02173; cyt_kin_arch; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..182
FT /note="Cytidylate kinase"
FT /id="PRO_0000132023"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 175..182
FT /note="NLHSALSH -> TYTRLCGIDLLNIYPE (in Ref. 1; CAA73486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20696 MW; CD5C42C3906377AD CRC64;
MKIIISGPPG SGKSSVAKIL SSKLSIKYVS AGLIFRDLAK RMNIDIVKLN KLAEDDFEID
KKIDLEMFKL IKSQDNVIIE SHIGGWLFHN LSDLSIYLRA PLDVRAKRIA SRDHISEDEA
IIQIIKRERS HRERFLRYYG IDILDLSVFD LVINTSYLLP EDVADIILGV ISRKNLHSAL
SH
