ID A0A0C2LHC6_9CYAN Unreviewed; 534 AA.
AC A0A0C2LHC6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Bifunctional pantoate ligase/cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
DE Includes:
DE RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_01349};
DE Short=PS {ECO:0000256|HAMAP-Rule:MF_01349};
DE EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_01349};
DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_01349};
DE AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01349};
DE Includes:
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_01349};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_01349};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_01349};
GN Name=panC/cmk {ECO:0000256|HAMAP-Rule:MF_01349};
GN ORFNames=SD81_32285 {ECO:0000313|EMBL:KIJ74036.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ74036.1};
RN [1] {ECO:0000313|EMBL:KIJ74036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ74036.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000256|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:0000256|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:0000256|ARBA:ARBA00001155, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|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:0000256|ARBA:ARBA00004990, ECO:0000256|HAMAP-Rule:MF_01349}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009427}.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000256|ARBA:ARBA00009256}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase
CC family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01349}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate
CC synthetase family. {ECO:0000256|HAMAP-Rule:MF_01349}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIJ74036.1}.
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DR EMBL; JXCB01000012; KIJ74036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2LHC6; -.
DR OrthoDB; 9773087at2; -.
DR UniPathway; UPA00028; UER00005.
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 CDD; cd00560; PanC; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 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 NCBIfam; TIGR00017; cmk; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR00018; panC; 1.
DR PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1.
DR PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR Pfam; PF02569; Pantoate_ligase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01349};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01349};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01349};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01349};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01349};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01349};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_01349};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000313|EMBL:KIJ74036.1}.
FT DOMAIN 312..530
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000259|Pfam:PF02224"
FT REGION 1..303
FT /note="Pantoate--beta-alanine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT REGION 304..534
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 79
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 79
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 172..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 178
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 209..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
SQ SEQUENCE 534 AA; 58785 MW; 5D7722A863B2971C CRC64;
MRLLRTVAAL RCYLAKHRFE NQLVDQPQPL PFEVTGRSKT AVGLVPTMGA LHEGHLSLIQ
RARDENATVI VSIFVNPLQF GPNEDYQRYP RTFDQDRLLC EQAGVNAIFA PTPEEVGVAE
KNIQESKVTQ VIPPSAMISG LCGRSRLGHF QGVTTIVTKL FNLVQPDRAY FGQKDGQQLA
IIKRLVADLN FPIEIVACPT VREASGLAIS SRNQYLTATQ KQQAAVLYSG LQKAQAAFKA
GERDAKALIA VVQQEVAMVS SVLVEYIELV EPNTLMLIEE KVQEEGMLAI AARLGSTRLI
DNTILRDRKP IIAIDGPAGA GKSTVARQVA ANLGLVYLDS GAMYRAVTWL VLQKGIALDD
ECAIAELADH CVIELTPSEN LQSPMRVWIN GTDVTQAIRT LEVTSKVSAV AAQTAVRQAL
VKQQHSWGKK GGLVAEGRDI GTHVFPDAEL KIFLTASVSE RARRRLQDFK KQGQPEVSLE
QMEKDIAERD WKDTTRKVSP LKKAPDAVEI KTDGLSVSQV TEQIVDYYQQ RLSQ
//
