PANCY_SYNY3
ID PANCY_SYNY3 Reviewed; 513 AA.
AC Q55074; P74087; Q55073;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
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}; Synonyms=panC/kcy;
GN OrderedLocusNames=sll1249;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9617794; DOI=10.1023/a:1005959200390;
RA So A.K.C., Espie G.S.;
RT "Cloning, characterization and expression of carbonic anhydrase from the
RT cyanobacterium Synechocystis PCC6803.";
RL Plant Mol. Biol. 37:205-215(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA86660.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U44896; AAA86660.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U44896; AAA86661.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18165.1; -; Genomic_DNA.
DR PIR; S75604; S75604.
DR AlphaFoldDB; Q55074; -.
DR SMR; Q55074; -.
DR IntAct; Q55074; 1.
DR STRING; 1148.1653250; -.
DR PaxDb; Q55074; -.
DR EnsemblBacteria; BAA18165; BAA18165; BAA18165.
DR KEGG; syn:sll1249; -.
DR eggNOG; COG0283; Bacteria.
DR eggNOG; COG0414; Bacteria.
DR InParanoid; Q55074; -.
DR OMA; IDHVFLM; -.
DR PhylomeDB; Q55074; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
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:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central.
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 CDD; cd00560; PanC; 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; 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; TIGR00018; panC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Ligase; Multifunctional enzyme;
KW Nucleotide-binding; Pantothenate biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..513
FT /note="Bifunctional pantoate ligase/cytidylate kinase"
FT /id="PRO_0000131992"
FT REGION 1..283
FT /note="Pantoate--beta-alanine ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT REGION 284..513
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 61
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 61
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 150..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 156
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
FT BINDING 187..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01349"
SQ SEQUENCE 513 AA; 55452 MW; 5A216A6E718A677B CRC64;
MVQVFRTIAG LQTYLRQAGR GKTVGLVPTM GSLHAGHGSL LKRAVAEMDL VVLSIFVNPL
QFGPGEDLEK YPRDFDGDRQ WAESLGVAVI FAPTVTDLGI DAKGDQTTVL PPPAMTEVLC
GAHRPGHFQG VATIVTKLFT IVCPDVAYFG AKDAQQLAII RRLVQDLNLT VTIRSCATVR
EESGLAMSSR NQYLSPIEKE QATVLYRSLQ AAQQRYRQGD RQVSALLTAT QDVLDAEPSV
QVQYLQLVEA DTLQPITGTL PDQNPVLMAI AAYVGSTRLI DNLVLNHRLP IIAIDGPAGA
GKSTVTRQVA DGLGLTYLDT GAMYRALAWL ILDQGIAPED EPAVAELTSG AEIELMPRPA
PQLTGVKVNG QDVSDAIRTP AVTQLVSTIA AQGAVRAKLL KLQRKYGDQG GIVAEGRDIG
TQVFPNAELK IFLTASVQER ARRRLKDFEA QGNQAVDLAQ LEADIAHRDH LDSTRAIAPL
QKAVDAVEII TDNLTIAEVV ETIIELYKKY NKG
