Reviewed, UniProtKB/Swiss-Prot Q318F2 (PANCY_PROM9)

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:	PMT9312_1682

Organism

Prochlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]

Taxonomic identifier

74546 [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)

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_0000239789
Regions
	Nucleotide binding	289 – 297	9	ATP By similarity
	Region	1 – 276	276	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	277 – 510	234	Cytidylate kinase HAMAP MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q318F2-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 3F9FC5D467800741	FASTA	510	58,205
	10 20 30 40 50 60 MKKVIIRKTE EIKNWRRNIN SDINFIPTMG NLHNGHKTLI STAKNANSNV NLVSIFVNPL 70 80 90 100 110 120 QFDNKSDLEN YPKTIDNDIK ISFENGADVI FIPSTEEIYP SDNKNITFLK APLELSSSLC 130 140 150 160 170 180 GLNRIGHFDG VCTVVYKLLN LIKPKNLYLG EKDWQQLLIL KNLVLTKKLD VAIKSIPTQR 190 200 210 220 230 240 DFDGIPLSSR NVHLSNNERK LIRFFSHELL VAKENFQQEK KINLKEIIQK LSAQKISIEY 250 260 270 280 290 300 LEHLHPYTLQ ESKVEDNISI LAGAIRCGET RLIDHVFLMK RSPIIAIDGP AGSGKSTVTQ 310 320 330 340 350 360 LIAKKLKLLY LDTGAMYRAL SWLLIKENID YKEEKKLQNI LKDISIVFKS NTNSQQDVFI 370 380 390 400 410 420 NNYCVTEEIR SQEISSIVSK ISSIKEVREF LVEEQRKIGE SGGLVAEGRD IGTTVFPDAE 430 440 450 460 470 480 LKIFLTASID ERAKRRKSDK KSKDSQEIDL HKLKELIKKR DFEDSNREIS PLIKANDAIE 490 500 510 IITDGCSINE VVDKIIDLYN DKIPKETQIR

References

[1]

"Complete sequence of Prochlorococcus marinus str. MIT 9312." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000111 Genomic DNA. Translation: ABB50743.1.
RefSeq	YP_398179.1.
3D structure databases
SMR	Q318F2. Positions 5-278, 279-503.
ModBase	Search...
Protein-protein interaction databases
STRING	Q318F2.
Genome annotation databases
GeneID	3766505.
GenomeReviews	Gene locus PMT9312_1682 in contig CP000111_GR.
KEGG	pmi:PMT9312_1682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
OMA	LGEKDWQ.
Enzyme and pathway databases
BioCyc	PMAR74546:PMT9312_1682-MONOMER.
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_PROM9

Accession

Primary (citable) accession number: Q318F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	December 6, 2005
Last modified:	February 9, 2010
This is version 30 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)