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Bifunctional pantoate ligase/cytidylate kinase [Includes: Cytidylate kinase (CK) (EC 2.7.4.14) (Cytidine monophosphate kinase) (CMP kinase); Pantothenate synthetase (PS) (EC 6.3.2.1) (Pantoate-activating enzyme) (Pantoate--beta-alanine ligase)]

 Q1PKA2_PROMR            Unreviewed;       509 AA.
Q1PKA2;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
22-NOV-2017, entry version 70.
RecName: Full=Bifunctional pantoate ligase/cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
Includes:
RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_01349};
Short=PS {ECO:0000256|HAMAP-Rule:MF_01349};
EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_01349};
AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_01349};
AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01349};
Includes:
RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
Short=CK {ECO:0000256|HAMAP-Rule:MF_01349};
EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_01349};
AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01349};
Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_01349};
Name=panC/ cmk {ECO:0000313|EMBL:ABE11150.1};
Synonyms=panC/cmk {ECO:0000256|HAMAP-Rule:MF_01349};
ORFNames=HF10-11H11_0007 {ECO:0000313|EMBL:ABE11150.1};
uncultured Prochlorococcus marinus clone HF10-11H11.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379375 {ECO:0000313|EMBL:ABE11150.1};
[1] {ECO:0000313|EMBL:ABE11150.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11150.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine
in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
{ECO:0000256|HAMAP-Rule:MF_01349}.
-!- FUNCTION: Displays a CMP kinase activity. {ECO:0000256|HAMAP-
Rule:MF_01349}.
-!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP +
diphosphate + (R)-pantothenate. {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00387728}.
-!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP.
{ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000256|SAAS:SAAS00643702}.
-!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
(R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000256|SAAS:SAAS00387774}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00573540}.
-!- SIMILARITY: In the C-terminal section; belongs to the cytidylate
kinase family. Type 1 subfamily. {ECO:0000256|HAMAP-
Rule:MF_01349}.
-!- SIMILARITY: In the N-terminal section; belongs to the pantothenate
synthetase family. {ECO:0000256|HAMAP-Rule:MF_01349}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01349}.
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EMBL; DQ366723; ABE11150.1; -; Genomic_DNA.
ProteinModelPortal; Q1PKA2; -.
UniPathway; UPA00028; UER00005.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
HAMAP; MF_00158; PanC; 1.
HAMAP; MF_01349; PanCY; 1.
InterPro; IPR003136; Cytidylate_kin.
InterPro; IPR011994; Cytidylate_kinase_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003721; Pantoate_ligase.
InterPro; IPR024894; Pantoate_ligase/cytidylate_kin.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF02224; Cytidylate_kin; 1.
Pfam; PF02569; Pantoate_ligase; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00017; cmk; 1.
TIGRFAMs; TIGR00018; panC; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00094328};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00094346};
Kinase {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00643704, ECO:0000313|EMBL:ABE11150.1};
Ligase {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00094334};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01349};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00094328};
Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00094356};
Transferase {ECO:0000256|HAMAP-Rule:MF_01349,
ECO:0000256|SAAS:SAAS00643704, ECO:0000313|EMBL:ABE11150.1}.
DOMAIN 284 497 Cytidylate_kin.
{ECO:0000259|Pfam:PF02224}.
NP_BIND 29 36 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}.
NP_BIND 149 152 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}.
NP_BIND 186 189 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}.
REGION 1 275 Pantoate--beta-alanine ligase.
{ECO:0000256|HAMAP-Rule:MF_01349}.
REGION 276 509 Cytidylate kinase. {ECO:0000256|HAMAP-
Rule:MF_01349}.
ACT_SITE 36 36 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_01349}.
BINDING 61 61 Beta-alanine. {ECO:0000256|HAMAP-
Rule:MF_01349}.
BINDING 61 61 Pantoate. {ECO:0000256|HAMAP-
Rule:MF_01349}.
BINDING 155 155 Pantoate. {ECO:0000256|HAMAP-
Rule:MF_01349}.
SEQUENCE 509 AA; 58244 MW; EEF5D77F1BB2E8F5 CRC64;
MKKVIIRTTE EIENWRRNIN SEINFIPTMG NLHNGHIKLI STAKNDNSNV NLVSIFINPL
QFDNKLDLEN YPKTIDNDIK ISFSNGADVI FIPSNEEIYP PNKNIKFLKA PIELSSALCG
LNRIGHFDGV CTVVYRLLNL IKPKNLYLGE KDWQQLLILK NLVLKNNLSV AIKSIPTQRD
FDGIPLSSRN INLSKNERKL IRFFSSELFE AKKNFQQEKK INLNEIIKKL SAKKISIEYL
EHLHPHTLQK ARFKDNISLL AGAIKCGETR LIDHVFLMKR RPIIAIDGPA GSGKSTVTKL
IAKKLKLLYL DTGAMYRALS WLILKEGIDY KKEKKLQNIL KDISIVFKSH TNSHQDVFIN
NRCVTEEIRS QEISSIVSKI SSIKEVRKFL VEEQRKIGKS GGLVAEGRDI GTTVFPHAEL
KIFLTASIDE RAKRRKSDTN SKDSQEIDLH TLKELIKKRD FEDSNREISP LIKANNAIEI
ITDGYSINEV VDKIIDLYYD KIPKETEIE


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