Q2JJ30 (PANCY_SYNJB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional pantoate ligase/cytidylate kinase

Including the following 2 domains:

1. Pantoate--beta-alanine ligase
   EC=6.3.2.1
   Alternative name(s):
   Pantoate-activating enzyme
   Pantothenate synthetase
2. 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:	CYB_2425

Organism

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321332 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_01349 ATP + (d)CMP = ADP + (d)CDP. HAMAP-Rule MF_01349
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule 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: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytidylate kinase activity Inferred from electronic annotation. Source: EC pantoate-beta-alanine ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349		PRO_0000239796
Regions
	Nucleotide binding	317 – 325	9	ATP By similarity
	Region	1 – 280	280	Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
	Region	281 – 542	262	Cytidylate kinase HAMAP-Rule MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q2JJ30 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: BE1BF4BB355F078A	FASTA	542	59,857
	10 20 30 40 50 60 MHWLRTVAAL REQVADWRGS TVGLVPTMGS LHEGHLSLIR RCRQECDHTV VSIFVNPLQF 70 80 90 100 110 120 GPNEDWDRYP RDEEGDRALC EAAGVDVVFA PDPQEMGADP ATGSDRTWVM PPESLLQTLC 130 140 150 160 170 180 APHRPGHFRG VATIVLQLLN LVQPQRAYFG QKDAQQLAII QRLVRDLQIP TTIVPCSTVR 190 200 210 220 230 240 EADGLACSSR NRYLSAAERQ VAAGLYRALR RGYDHWQAGD PSAEGILAAA RAELEHTPEL 250 260 270 280 290 300 QLQYLELVDP QTLQPLPRVE DKGLLAIAAY VGQTRLIDNL LLSPEQGDPL PERVQHAAPP 310 320 330 340 350 360 SSGTTSPPRR PLIAIDGPAG AGKSTVARAV AAQLQLLYLD TGAMYRAITW LALQRGIPLD 370 380 390 400 410 420 DAEQLTQLAA QTQLTLQSGT SSTEPTRIWA DGEEITQAIR SPEVTRWVSH VAAVPGVRQE 430 440 450 460 470 480 LVKRQRSIGR DGGAVLEGRD IGTHVFPDAE LKVFLTASVG ERAQRRQHQL QAQGQMVPLE 490 500 510 520 530 540 ELKAQIEQRD RRDSERLISP LRPAPDAILI DTDHLSQSEV QDKIVMLYRQ LLERSGPARL DQ

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000240 Genomic DNA. Translation: ABD03359.1.
RefSeq	YP_478622.1. NC_007776.1.
3D structure databases
ProteinModelPortal	Q2JJ30.
ModBase	Search...
Protein-protein interaction databases
STRING	321332.CYB_2425.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD03359; ABD03359; CYB_2425.
GeneID	3901394.
KEGG	cyb:CYB_2425.
PATRIC	23807200. VBISynSp29577_2425.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0283.
HOGENOM	HOG000233355.
KO	K13799.
OMA	LGEKDWQ.
ProtClustDB	PRK13477.
Enzyme and pathway databases
UniPathway	UPA00028; UER00005.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_01349. PanCY.
InterPro	IPR004821. Cyt_trans-like. IPR003136. Cytidylate_kin. IPR011994. Cytidylate_kinase_dom. IPR003721. Pantoate_ligase. IPR024894. Pantoate_ligase/cytidylate_kin. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfam	PF02224. Cytidylate_kin. 1 hit. PF02569. Pantoate_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00017. cmk. 1 hit. TIGR00125. cyt_tran_rel. 1 hit. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_SYNJB

Accession

Primary (citable) accession number: Q2JJ30

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program