A2CBX2 (PANCY_PROM3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional pantoate ligase/cytidylate kinase

Including the following 2 domains:

1. Pantothenate synthetase
   Short name=PS
   EC=6.3.2.1
   Alternative name(s):
   Pantoate--beta-alanine ligase
   Pantoate-activating enzyme
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:	P9303_22471

Organism

Prochlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]

Taxonomic identifier

59922 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus › Prochlorococcus marinus

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_01349 Displays a CMP kinase activity By similarity.
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 – 488	488	Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349		PRO_0000333298
Regions
	Nucleotide binding	1 – 8	8	ATP By similarity
	Nucleotide binding	125 – 128	4	ATP By similarity
	Nucleotide binding	162 – 165	4	ATP By similarity
	Region	1 – 251	251	Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
	Region	252 – 488	237	Cytidylate kinase HAMAP-Rule MF_01349
Sites
	Active site	8	1	Proton donor By similarity
	Binding site	36	1	Beta-alanine By similarity
	Binding site	36	1	Pantoate By similarity
	Binding site	131	1	Pantoate By similarity
	Binding site	154	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2CBX2 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: BF8216EDE9F518EC	FASTA	488	53,156
	10 20 30 40 50 60 MGALHRAHGQ LIKSVQGFGS LQPAAVLVSV FVNPLQFGPA EDFDSYPRDL EADCELASRS 70 80 90 100 110 120 GASALWAPSV DQVFPGGASS QFRIQVPSHL QAHLCGAIRP GHFDGVVTVV ARLLALVRPE 130 140 150 160 170 180 VLVLGEKDWQ QLVILRHLVA QLGLPVRVHG VATVRDDDGL ACSSRNRYLM TQQRQQALAL 190 200 210 220 230 240 PQLLARAARE SQDGRAVDLA GLRCAWEQLG LEVEYVETVD AFNLQPLHAG RKLCLLAAAV 250 260 270 280 290 300 RCGETRLIDH TFLMSRQPIV AIDGPAGAGK STVTRAFAER LGLLYLDTGA MYRAVTWLTQ 310 320 330 340 350 360 QHDVDPHDPV AVKTILENLE LELEPSQSGP QKVRINGHDV TEAIRSPEVT SSVSVVAAHG 370 380 390 400 410 420 CVRKALTAQQ QRMGVRGGLV AEGRDIGTAV FPDAELKVFL TASPAERARR RALDLDNRGF 430 440 450 460 470 480 PVPDLAELET QIEERDRMDS TREVAPLRQA EDATELISDG MSIEEVIETL IDLFRVQVPE EVWPTPGS

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000554 Genomic DNA. Translation: ABM78982.1.
RefSeq	YP_001018247.1. NC_008820.1.
3D structure databases
ProteinModelPortal	A2CBX2.
ModBase	Search...
Protein-protein interaction databases
STRING	59922.P9303_22471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM78982; ABM78982; P9303_22471.
GeneID	4778424.
KEGG	pmf:P9303_22471.
PATRIC	23002033. VBIProMar17757_2311.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0283.
HOGENOM	HOG000233355.
KO	K13799.
OMA	LGEKDWQ.
ProtClustDB	PRK13477.
Enzyme and pathway databases
BioCyc	PMAR59922:GH54-2353-MONOMER.
UniPathway	UPA00028; UER00005.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_01349. PanCY.
InterPro	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. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_PROM3

Accession

Primary (citable) accession number: A2CBX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program