Reviewed, UniProtKB/Swiss-Prot Q0ICW2 (PANCY_SYNS3)

Names and origin

Protein names

Recommended name:
    Bifunctional pantoate ligase/cytidylate kinase
Including the following 2 domains:
    1- Recommended name:
            Pantothenate synthetase
                Short name=PS
              EC=6.3.2.1
        Alternative name(s):
            Pantoate--beta-alanine ligase
            Pantoate-activating enzyme
    2- Recommended name:
            Cytidylate kinase
                Short name=CK
              EC=2.7.4.14
        Alternative name(s):
            Cytidine monophosphate kinase
              Short name=CMP kinase

Gene names

Name:	panC/cmk
Ordered Locus Names:	sync_0483

Organism

Synechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]

Taxonomic identifier

64471 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. Displays a CMP kinase activity By similarity.
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_01349 ATP + (d)CMP = ADP + (d)CDP. HAMAP MF_01349
Pathway	Cofactor biosynthesis; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: step 1/1. HAMAP MF_01349
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the pantothenate synthetase family. In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyrimidine nucleotide metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP cytidylate kinase activity Inferred from electronic annotation. Source: HAMAP pantoate-beta-alanine ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333300
Regions
	Nucleotide binding	7 – 14	8	ATP By similarity
	Nucleotide binding	130 – 133	4	ATP By similarity
	Nucleotide binding	167 – 170	4	ATP By similarity
	Region	1 – 258	258	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	259 – 494	236	Cytidylate kinase HAMAP MF_01349
Sites
	Active site	14	1	Proton donor By similarity
	Binding site	41	1	Beta-alanine By similarity
	Binding site	41	1	Pantoate By similarity
	Binding site	136	1	Pantoate By similarity
	Binding site	159	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0ICW2-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: E7EDD078F93465E3	FASTA	494	53,594
	10 20 30 40 50 60 MHFVPTMGGL HHGHASLISA ASCHKSGDVE TLVSVFVNPL QFGPNEDFAR YPRTFEADCE 70 80 90 100 110 120 LAELSGASAI WCPDESQIYP GGSAESWRIQ APKSLQSRLC GSTRPGHFDG VVTVVCRLLA 130 140 150 160 170 180 LAKPHQLFLG EKDWQQLTIL RRMVLDLGLA VRVRGVPTVR DGDGLASSSR NRYLNAQQRQ 190 200 210 220 230 240 QGVLFAQVLS DARSACLHGG TALKPGEVKR RLEEVGLSVE YVDVVDPWFL QPSKSNQSSL 250 260 270 280 290 300 TLLAAAVRCG STRLIDHAFL MTRSPLVAID GPAGAGKSTV TRAFAERLGL VYLDTGAMYR 310 320 330 340 350 360 AVTWLVLEQG GDPGDSEAVD LVLNDLKVEL EPLQQGVQVV RVNGHEVTDA IRDPRVTASV 370 380 390 400 410 420 SAVASHACVR AAMTAQQQRM GKAGGLVAEG RDIGTAVFPD AELKVFLTAT PKERARRRAL 430 440 450 460 470 480 DLEARGHEVP ALPELEAQIV ERDRLDSTRE VAPLLQADDA IELISDGMSI DQVIDALEDL 490 FRRRVGEEVW PTPV

References

[1]

"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment." Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T. Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed: 16938853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000435 Genomic DNA. Translation: ABI45138.1.
RefSeq	YP_729710.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4260685.
GenomeReviews	Gene locus sync_0483 in contig CP000435_GR.
KEGG	syg:sync_0483.
TIGR	sync_0483.
Phylogenomic databases
HOGENOM	Q0ICW2.
OMA	Q0ICW2. LGEKDWQ.
Family and domain databases
HAMAP	MF_01349. [Tree]
InterPro	IPR003136. Cytidylate_kin. IPR011994. Cytidylate_kin_d. IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR21299:SF1. Pantoate_ligase. 1 hit.
Pfam	PF02224. Cytidylate_kin. 1 hit. PF02569. Pantoate_ligase. 1 hit. [Graphical view]
ProDom	PD000657. Adenylate_kin. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00017. cmk. 1 hit. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_SYNS3

Accession

Primary (citable) accession number: Q0ICW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 3, 2006
Last modified:	June 16, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)