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PANCY_PARMW
ID   PANCY_PARMW             Reviewed;         501 AA.
AC   Q7U4P0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Bifunctional pantoate ligase/cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_01349};
DE   Includes:
DE     RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_01349};
DE              Short=PS {ECO:0000255|HAMAP-Rule:MF_01349};
DE              EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01349};
DE     AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_01349};
DE     AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01349};
DE   Includes:
DE     RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_01349};
DE              Short=CK {ECO:0000255|HAMAP-Rule:MF_01349};
DE              EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_01349};
DE     AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01349};
DE              Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_01349};
GN   Name=panC/cmk {ECO:0000255|HAMAP-Rule:MF_01349};
GN   OrderedLocusNames=SYNW2027;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC       an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_01349}.
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group from ATP to
CC       either CMP or dCMP to form CDP or dCDP and ADP, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_01349}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01349};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01349};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01349};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01349}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01349}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate
CC       synthetase family. {ECO:0000255|HAMAP-Rule:MF_01349}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase
CC       family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01349}.
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DR   EMBL; BX569694; CAE08542.1; -; Genomic_DNA.
DR   RefSeq; WP_011128885.1; NC_005070.1.
DR   AlphaFoldDB; Q7U4P0; -.
DR   SMR; Q7U4P0; -.
DR   STRING; 84588.SYNW2027; -.
DR   EnsemblBacteria; CAE08542; CAE08542; SYNW2027.
DR   KEGG; syw:SYNW2027; -.
DR   eggNOG; COG0283; Bacteria.
DR   eggNOG; COG0414; Bacteria.
DR   HOGENOM; CLU_037427_0_0_3; -.
DR   OMA; IDHVFLM; -.
DR   OrthoDB; 1661843at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000001422; 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:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
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; 3.30.1300.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   HAMAP; MF_01349; PanCY; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR024894; Pantoate_ligase/cytidylate_kin.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Pantothenate biosynthesis; Transferase.
FT   CHAIN           1..501
FT                   /note="Bifunctional pantoate ligase/cytidylate kinase"
FT                   /id="PRO_0000239799"
FT   REGION          1..264
FT                   /note="Pantoate--beta-alanine ligase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   REGION          265..501
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   ACT_SITE        32
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         25..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         55
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         55
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         144..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         150
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT   BINDING         181..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ   SEQUENCE   501 AA;  53427 MW;  1EA5EFDEE595D85F CRC64;
     MLSTQAELAA FHSGLGQPLQ FVPTMGGLHQ GHGELIRRAA EQGPVLVSVF VNPLQFAPGE
     DFERYPRSLE ADLALADRYG AAALWTPTVQ TIYPDGATAD SARQAPAALQ QHLCGADRPG
     HFDGVVTVVA RLLELTRPAG LWLGEKDWQQ LVILRQLVAD LVLPVKIHGV ATVREADGLA
     LSSRNQYLSA AQRLQAAALP AALRAADGTT PLDVTRSRLS AAGLEVEYVE RVDPQSLQPC
     GSETALSLLA AAVRCGTTRL IDHSFLMTRQ PLVAIDGPAG AGKSTVTRAF AERLGLIYLD
     TGAMYRAVTW LVQQQGVEPG DAAAVDALLR ALDLQLQSLP GGGQQVMVNG EDVSQAIRSP
     EVTGSVSVVA AHRCVRQALT TQQKAMGAKG GLVAEGRDIG SAVFPDADLK VFLTATVAER
     ARRRALDLEQ RGFPVQERSE LEAQIAERDH LDSTREEAPL VQAIDAVELV TDGMSIDAVI
     DALVEQFRAR VPEEAWPTPA G
 
 
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