ID A0A0T7BUA1_9CYAN Unreviewed; 530 AA.
AC A0A0T7BUA1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=IJ00_16420 {ECO:0000313|EMBL:AKG22646.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG22646.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG22646.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG22646.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
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; CP011382; AKG22646.1; -; Genomic_DNA.
DR RefSeq; WP_035154638.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7BUA1; -.
DR STRING; 1337936.IJ00_16420; -.
DR KEGG; calh:IJ00_16420; -.
DR eggNOG; COG0283; Bacteria.
DR eggNOG; COG0414; Bacteria.
DR OrthoDB; 9773087at2; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000065745; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000313|EMBL:AKG22646.1}.
FT DOMAIN 309..526
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000259|Pfam:PF02224"
FT REGION 1..300
FT /note="Pantoate--beta-alanine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT REGION 301..530
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT ACT_SITE 53
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 77
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 77
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 170..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 176
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
FT BINDING 207..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349"
SQ SEQUENCE 530 AA; 58422 MW; CFFB5432A5AEE0EE CRC64;
MRLLTTVAAL RCYLAKRRLE SQEPEPPLQF DITAWTSTAV GLVPTMGALH QGHLSLVERA
RQENATVIVS IFVNPLQFGP NEDYQRYPRT LEEDRQWCET AGVDAIFAPT PEEMGIMEKN
IQETRVTQVI PPSAMISGLC GRSRLGHFQG VATIVTKLFN LVQPDRAYFG QKDGQQLAII
KRLVADLDLP IDIVACPTVR EASGLALSSR NQYLTATEKS QAAVLYRGLQ QAVTLFRAGV
RTANDLIAAV QQEVATISNL LVEYIELVEP NTLLPLETIQ EEGMLAIAAR LGSTRLIDNT
ILRDRQPIIA IDGPAGAGKS TVARQVAANL GLVYLDTGAM YRAVTWLVLQ AGIPTDDECA
IAELVSKSVI ELAPSHDLQF PVQVYINGHN VTPEIRTREV TAHVSAIAAQ TSVRQALVKQ
QQMWGKKGGL VAEGRDIGTC VFPDAEVKIF LTASVQERAR RRLQDFHNQG QPVMTLEELE
KDIAERDWKD SNRQVSPLRK AVDAVEMITD GLSIPEVTAK IVDYYQKQLS
//
