ID PANCY_PROMA Reviewed; 519 AA. AC Q7V9S8; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 03-APR-2007, entry version 21. DE Bifunctional pantoate ligase/cytidylate kinase [Includes: Pantoate-- DE beta-alanine ligase (EC 6.3.2.1) (Pantothenate synthetase) (Pantoate- DE activating enzyme); Cytidylate kinase (EC 2.7.4.14) (CK) (Cytidine DE monophosphate kinase) (CMP kinase)]. GN Name=panC/cmk; OrderedLocusNames=Pro_1746; OS Prochlorococcus marinus. OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=1219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP 1375 / SS120; RX MEDLINE=22810154; PubMed=12917486; DOI=10.1073/pnas.1733211100; RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., RA Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., RA Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P., RA Wolf Y.I., Hess W.R.; RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, RT a nearly minimal oxyphototrophic genome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003). CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + CC diphosphate + (R)-pantothenate. CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC -!- PATHWAY: Cofactor biosynthesis; pantothenate biosynthesis; CC pantothenate from beta-alanine and pantoate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate CC synthetase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate CC kinase family. Type 1 subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017126; AAQ00790.1; -; Genomic_DNA. DR HSSP; P23863; 1KDO. DR GenomeReviews; AE017126_GR; Pro_1746. DR KEGG; pma:Pro1746; -. DR BioCyc; PMAR167539:PRO1746-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:HAMAP. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:HAMAP. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:HAMAP. DR HAMAP; MF_01349; -; 1. DR InterPro; IPR011769; Ad_Ct_kin_N. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kin_d. DR InterPro; IPR003721; Pantoate_ligase. DR Pfam; PF02224; Cytidylate_kin; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR ProDom; PD000657; Adenylate_kin; 1. DR TIGRFAMs; TIGR00017; cmk; 1. DR TIGRFAMs; TIGR00018; panC; 1. KW ATP-binding; Complete proteome; Kinase; Ligase; KW Multifunctional enzyme; Nucleotide-binding; Pantothenate biosynthesis; KW Transferase. FT CHAIN 1 519 Bifunctional pantoate ligase/cytidylate FT kinase. FT /FTId=PRO_0000239790. FT NP_BIND 295 303 ATP (By similarity). FT REGION 1 282 Pantoate--beta-alanine ligase. FT REGION 283 519 Cytidylate kinase. SQ SEQUENCE 519 AA; 58064 MW; 268B7AFEF6EA074C CRC64; MNLTILRTKT ALEDWCRQKH NHEINFVPTM GGLHQGHQEL IKTARSFCKR KHSSQVLVSI FINPLQFDLE EDFKKYPRTF ENDCKIAYEA GANAIWAPSF ESVFPNGEEA HFKIQVPFSL NKYLCGASRE GHFDGVATVV VRLLALVRPN RIFLGEKDWQ QLVILRQLIN DLGLPVLIHS IPTKRDQDGL PCSSRNVNLS KEERKKVVAL PAVLQQAAQA FQENKPINLN NMKTTLEEHD LKVEYLETVD LKNLNPVNHD ESKLCLLAAA VHCGNTRLID HGFLMKRNPI VAIDGPAGAG KSTVTKKFAQ KLGLIYLDTG AMYRAVTWLI QENNIDPQNS SELELILNDI NLDICLSNTG NQQVLINGKD ITTLIRSPTV TSQVSLVAAI GSVREKLTSQ QKELGSKGGL VAEGRDIGTA VFPDAELKIF LTATAQERAK RRAIDLKKQG FSTPSLSELE KQIKERDRLD SSREIAPLSK AKDAQELITD GMNIEEVVEL LINIFREKIP QEVWPTNAT //