Reviewed, UniProtKB/Swiss-Prot A8G795 (PANCY_PROM2)

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:	P9215_18631

Organism

Prochlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]

Taxonomic identifier

93060 [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: 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 – 510	510	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333296
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)
	A8G795-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: BC3128378F890BF4	FASTA	510	58,304
	10 20 30 40 50 60 MKKVIIRKTE EIENWKRNIN NEINFIPTMG NLHNGHIKLI STAKNDNSNV NLVSIFINPL 70 80 90 100 110 120 QFDNKLDLEN YPKTIDNDIK ISFSNGADAI FIPSNEDIYP PNNKNIKFLK APIELSSALC 130 140 150 160 170 180 GLNRIGHFDG VCTVVYRLLN LIKPKNLYLG EKDWQQLLIL KNLVLKEKLN VAIKSIPTQR 190 200 210 220 230 240 DFDGIPLSSR NVHLSKNERK LIRFFSSELL EAKKNFQQEK NINLNEIIKK LSAKKISIEY 250 260 270 280 290 300 LEHLHPHTLQ KARLEDNISL LAGAIRCGET RLIDHVFLMK RRPIIAIDGP AGSGKSTVTK 310 320 330 340 350 360 LIAKKLKLLY LDTGAMYRAL SWLLLKENID YKKEKKLLNI FKDISIVFKS NTNSHQDVYV 370 380 390 400 410 420 NNCCVTEEIR SQKISSIVSK ISSIKEVRKF LVEEQRKIGE SGGLVAEGRD IGTTVFPNAE 430 440 450 460 470 480 LKIFLTASID ERAKRRKSDK QSKDSQEIDL DTLKELIEKR DFEDSNREIS PLIKANDAIE 490 500 510 IISDGYTINE VVDKIIDLYN DKIPKETEIK

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	CP000825 Genomic DNA. Translation: ABV51476.1.
RefSeq	YP_001485062.1.
3D structure databases
SMR	A8G795. Positions 5-278, 279-503.
ModBase	Search...
Protein-protein interaction databases
STRING	A8G795.
Genome annotation databases
GeneID	5615083.
GenomeReviews	Gene locus P9215_18631 in contig CP000825_GR.
KEGG	pmh:P9215_18631.
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.
ProtoNet	Search...

Entry information

Entry name

PANCY_PROM2

Accession

Primary (citable) accession number: A8G795

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 13, 2007
Last modified:	February 9, 2010
This is version 17 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)