ID A0A1Y0RRA7_9CYAN Unreviewed; 534 AA.
AC A0A1Y0RRA7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BZZ01_30785 {ECO:0000313|EMBL:ARV62432.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV62432.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV62432.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV62432.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) 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}.
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DR EMBL; CP019636; ARV62432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RRA7; -.
DR KEGG; ncn:BZZ01_30785; -.
DR OrthoDB; 9773087at2; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000196302; 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 CDD; cd02019; NK; 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; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR PANTHER; PTHR21299:SF1; 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 Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01349}.
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; 59015 MW; F7F4EEE1DCBA46BD CRC64;
MRLLRTVAAL RCYLAKHRFE NQLVDQAHSW PFEVTARSKT ALGLVPTMGA LHEGHLSLIQ
QARQENATVI VSIFVNPLQF SPNEDYQRYP RTLEQDRLLC EKTGVDAIFA PSPEEMGVLE
KNIQESKVTQ VIPPSAMISG LCGRSRLGHF QGVATIVTKL FNLVQPDRAY FGQKDGQQLA
LIKRLVADLN FPIEIVACPT VREASGLALS SRNQYLTATQ KQQAAALYQG LQKAEAAFRA
GERDAKALVA VVQQEVAMFS SVLVEYIELV EANTLMPIEE KIEEEAMLAI AARLGSTRLI
DNVILRDRQP IIAIDGPAGA GKSTVARQVA AKLGLVYLDT GAMYRSVTWL VLQKGIALDD
ECAIAELANH CVIELAPSKD LQTPVQVWIN DIDVTQAIRS LEVTSKVSAI AAQSAVRQAL
VKQQQRWGKK GGLVAEGRDI GTQVFPDAEV KIFLTASVSE RARRRQQDFQ KQGQSEVSLE
QLEKDIAERD WKDSTRKVSP LQKAADAVEI QTDGMSISQV TEQIVDYYQQ RLSQ
//
