A3PF80 (PANCY_PROM0) 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:	P9301_17821

Organism

Prochlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP]

Taxonomic identifier

167546 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	510 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 MF_01349 Displays a CMP kinase activity By similarity. HAMAP MF_01349
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 HAMAP MF_01349.
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-KW
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 – 510	510	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333297
Regions
	Nucleotide binding	29 – 36	8	ATP By similarity
	Nucleotide binding	150 – 153	4	ATP By similarity
	Nucleotide binding	187 – 190	4	ATP By similarity
	Region	1 – 276	276	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	277 – 510	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	156	1	Pantoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3PF80 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: E82DF93842EDC030	FASTA	510	58,445
	10 20 30 40 50 60 MKKVIIRKTE EIENWRRNIN SEINFIPTMG NLHDGHIKLI STAKNDNSNV NLVSIFINPL 70 80 90 100 110 120 QFDNKLDLEN YPQTIDNDIK ISFSNGADAI FIPSYEDIYP PNNKNIKFLK APKELSSALC 130 140 150 160 170 180 GLNRIGHFDG VCTVVYRLLN LIKPKNLYLG EKDWQQLLIL KNLVLRKNLN VAIRSIPTQR 190 200 210 220 230 240 DFDGIPLSSR NVHLSKNERK LISFFSSELL EAKKIFQQDK KINLNQIIKK LSAKKISVEY 250 260 270 280 290 300 LEHLHPHTLQ KARPEDNISL LAGAIRCGET RLIDHVFLMK RRPIIAIDGP AGSGKSTVTK 310 320 330 340 350 360 LIAKKLNLLY LDTGAMYRAL SWLIIKESVD YKIEKKLQNI LKDISIFFKS NTNSHQDVYV 370 380 390 400 410 420 NNYCVTKEIR SQKISSIVSK ISSIKEVRKF LVAEQRKIGE SGGLVAEGRD IGTTVFPHAE 430 440 450 460 470 480 LKIFLTASID ERAKRRKYDK NSKDSQEIDL YTLKELIKKR DFEDSNREIS PLIKANDAIE 490 500 510 IITDGYTIDE VVDKIIDLYN DRIPKETEIK

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]. Strain: MIT 9301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000576 Genomic DNA. Translation: ABO18405.1.
RefSeq	YP_001092006.1. NC_009091.1.
3D structure databases
ProteinModelPortal	A3PF80.
ModBase	Search...
Protein-protein interaction databases
STRING	A3PF80.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4911848.
GenomeReviews	Gene locus P9301_17821 in contig CP000576_GR.
KEGG	pmg:P9301_17821.
PATRIC	22997073. VBIProMar103344_1706.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
OMA	LGEKDWQ.
PhylomeDB	A3PF80.
ProtClustDB	PRK13477.
Enzyme and pathway databases
BioCyc	PMAR167546:P9301ORF_1818-MONOMER.
Family and domain databases
HAMAP	MF_01349. PanCY. [Tree]
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]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K13799.
PANTHER	PTHR21299:SF2. Cytidylate_kin. 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_PROM0

Accession

Primary (citable) accession number: A3PF80

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program