Reviewed, UniProtKB/Swiss-Prot A2C536 (PANCY_PROM1)

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:	NATL1_20401

Organism

Prochlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP]

Taxonomic identifier

167555 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	516 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: 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 – 516	516	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333299
Regions
	Nucleotide binding	29 – 36	8	ATP By similarity
	Nucleotide binding	153 – 156	4	ATP By similarity
	Nucleotide binding	190 – 193	4	ATP By similarity
	Region	1 – 279	279	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	280 – 516	237	Cytidylate kinase HAMAP MF_01349
Sites
	Active site	36	1	Proton donor By similarity
	Binding site	64	1	Beta-alanine By similarity
	Binding site	64	1	Pantoate By similarity
	Binding site	159	1	Pantoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2C536-1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 6F1E35E3BFD96C4D	FASTA	516	58,348
	10 20 30 40 50 60 MVRKIFQTNA ELKDWLSEQN SAIIFIPTMG GLHPGHQYLI QKAKERKTNT NQIILVSIFV 70 80 90 100 110 120 NPLQFSKGED FKKYPRNINR DAELAFSAGA DAIWAPDYDE VFPGGADSHF KIEVPKTLHN 130 140 150 160 170 180 QLCGAERKGH FDGVATVIIR LIKIIKPKKL VLGEKDWQQL IIIRKLFQEL SIPVKIESYS 190 200 210 220 230 240 TQRDQSGFAY SSRNSYLSDS ERVNAQSLPN AIKEAKTEFD KGKVINLTKI ASIFKENNLK 250 260 270 280 290 300 IEYLKIVDPF SLKETENINR LCLLAVAVKC GSTRLIDHTF LMHRKPIIAI DGPAGAGKST 310 320 330 340 350 360 VTKAFAKKLG FIYLDTGAMY RAVTWLIISN SIDPNDQVEI KNILKDSKLE FKSSSFVEQK 370 380 390 400 410 420 IFINNIDVTE KIRSPKVTSM VSEIAKQQFV RELLTRKQQV IGNNGGLVAE GRDIGTAVFP 430 440 450 460 470 480 DADLKIFLTA SPTERAKRRA LDLHKRGYEF SSIEDLEKEI KERDKKDSER KIAPLKKAQD 490 500 510 AIELVTDGMN IEDVLKELID IFRSKIPEEV WPTPNS

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
EMBL GenBank DDBJ	CP000553 Genomic DNA. Translation: ABM76596.1.
RefSeq	YP_001015860.1.
3D structure databases
SMR	A2C536. Positions 4-281, 284-506.
ModBase	Search...
Protein-protein interaction databases
STRING	A2C536.
Genome annotation databases
GeneID	4779871.
GenomeReviews	Gene locus NATL1_20401 in contig CP000553_GR.
KEGG	pme:NATL1_20401.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
OMA	LGEKDWQ.
Family and domain databases
HAMAP	MF_01349. PanCY. [Tree]
InterPro	IPR003136. Cytidylate_kin. IPR011994. Cytidylate_kinase_dom. 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]
TIGRFAMs	TIGR00017. cmk. 1 hit. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_PROM1

Accession

Primary (citable) accession number: A2C536

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 20, 2007
Last modified:	February 9, 2010
This is version 23 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)