Reviewed, UniProtKB/Swiss-Prot Q46IM3 (PANCY_PROMT)

Names and origin

Protein names

Recommended name:
    Bifunctional pantoate ligase/cytidylate kinase
Including the following 2 domains:
    1- Recommended name:
            Pantoate--beta-alanine ligase
              EC=6.3.2.1
        Alternative name(s):
            Pantothenate synthetase
            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:	PMN2A_1165

Organism

Prochlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]

Taxonomic identifier

59920 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: 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 – 516	516	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000239793
Regions
	Nucleotide binding	292 – 300	9	ATP By similarity
	Region	1 – 279	279	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	280 – 516	237	Cytidylate kinase HAMAP MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q46IM3-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 3980DA9C3BFB07FA	FASTA	516	58,289
	10 20 30 40 50 60 MVRKIFQTNA ELKDWLSGQN SAIIFIPTMG GLHPGHQYLI QKAKEKKTNT NQIILVSIFV 70 80 90 100 110 120 NPLQFSKGED FKKYPRNIKR DAELAFSAGA DAIWAPEYDE VFPGGADSHF KIEVPKTLHN 130 140 150 160 170 180 QLCGAERKGH FDGVATVIIR LIKIIKPKKL ILGEKDWQQL IIIRKLFQEL SIPVKIESYS 190 200 210 220 230 240 TQRDQSGFAY SSRNSYLSDS ERVNAQSLPN AIKEAKTEFD KGKVINLTKI ASIFKENNLK 250 260 270 280 290 300 IEYLKIVDPF SLKETENINR LCLLAIAVKC GSTRLIDHTF LMHRKPIIAI DGPAGAGKST 310 320 330 340 350 360 VTKAFAKKLG FIYLDTGAMY RAVTWLIISN SIDPNDQAEI KNILKDSKLE FKNSSFVEQK 370 380 390 400 410 420 IFINNIDVTE KIRSPQVTSM VSEIAKQQFV REVLTRKQQV 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
EMBLGenBankDDBJ	CP000095 Genomic DNA. Translation: AAZ58655.1.
RefSeq	YP_292358.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3606556.
GenomeReviews	Gene locus PMN2A_1165 in contig CP000095_GR.
KEGG	pmn:PMN2A_1165.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q46IM3.
OMA	Q46IM3. LGEKDWQ.
Enzyme and pathway databases
BioCyc	PMAR59920:PMN2A_1165-MON.
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. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_PROMT

Accession

Primary (citable) accession number: Q46IM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	September 13, 2005
Last modified:	June 16, 2009
This is version 25 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)