Reviewed, UniProtKB/Swiss-Prot A2BTH1 (PANCY_PROMS)

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:	A9601_17991

Organism

Prochlorococcus marinus (strain AS9601) [Complete proteome] [HAMAP]

Taxonomic identifier

146891 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	509 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; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: 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 – 509	509	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333295
Regions
	Nucleotide binding	29 – 36	8	ATP By similarity
	Nucleotide binding	149 – 152	4	ATP By similarity
	Nucleotide binding	186 – 189	4	ATP By similarity
	Region	1 – 275	275	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	276 – 509	234	Cytidylate kinase HAMAP MF_01349
Sites
	Active site	36	1	Proton donor By similarity
	Binding site	61	1	Beta-alanine By similarity
	Binding site	61	1	Pantoate By similarity
	Binding site	155	1	Pantoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2BTH1-1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: AE119B900F9AC659	FASTA	509	58,242
	10 20 30 40 50 60 MKKLIIRKTE EIENWRKDID SEINFIPTMG NLHDGHIKLI STAKNDNSNI NLVSIFINPL 70 80 90 100 110 120 QFDNKLDLEN YPKTIDNDIN ISFSNGADAI FIPSNEDIYP PNNNISFLKA PIELSSALCG 130 140 150 160 170 180 LNRIGHFDGV CTVVYRLLNL IKPKNLYLGE KDWQQLLILK NLVLRKKLNI AIKSIPTQRD 190 200 210 220 230 240 FDGIPLSSRN VHLSKNERKL ISFFSRELLE AKKNFQKEKK INLKEIIKKL SEKKISIEYL 250 260 270 280 290 300 EHLHPYTLQK AKIEDNISLL AGAIRCGETR LIDHVFLMKR RPIIAIDGPA GSGKSTVTKL 310 320 330 340 350 360 IAKKLKLLYL DTGAMYRALS WLIIKENIDF KKENKLQNIL KDISIVFKSN TSSHQDVYVN 370 380 390 400 410 420 NYCVTEEIRS QKISSIVSKI SSIKEVREFL VEEQRKIGES GGLVAEGRDI GTTVFPHAEL 430 440 450 460 470 480 KIFLTASIDE RAKRRKSDKN SKDLQEIDLH KLKELIKQRD SEDSNRKISP LIKANDAIEI 490 500 ITDGYSINEV VDKIIDLYND KIPKESEIK

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000551 Genomic DNA. Translation: ABM71082.1.
RefSeq	YP_001010189.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A2BTH1.
Genome annotation databases
GeneID	4718534.
GenomeReviews	Gene locus A9601_17991 in contig CP000551_GR.
KEGG	pmb:A9601_17991.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	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.
ProtoNet	Search...

Entry information

Entry name

PANCY_PROMS

Accession

Primary (citable) accession number: A2BTH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 20, 2007
Last modified:	November 3, 2009
This is version 21 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)