Q7UZR6 (PANCY_PROMP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional pantoate ligase/cytidylate kinase

Including the following 2 domains:

1. Pantoate--beta-alanine ligase
   EC=6.3.2.1
   Alternative name(s):
   Pantoate-activating enzyme
   Pantothenate synthetase
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:	PMM1590

Organism

Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]

Taxonomic identifier

59919 [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: 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_0000239792
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)
	Q7UZR6 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 315DC94E014CBDF8	FASTA	510	58,295
	10 20 30 40 50 60 MNKIIIRKTE DLKEWRRNLK CDINFIPTMG NLHDGHQKLI STAQSSNCNT NLLSIFVNPL 70 80 90 100 110 120 QFDSKEDLKS YPKTVDKDIE IAFSNGADAI FIPNVTDIYP KKNKSISYLK ASKELSSALC 130 140 150 160 170 180 GLTRVGHFDG VCTVVYRLLK LIQPKNLFLG EKDWQQLLII KNLIEEKKFN IKIIPVPTQR 190 200 210 220 230 240 DSDGVPFSSR NKHLSKSERK SLKLFSNELE NAKIIFKKDK RIDLKQLTNK LKSKNISIEY 250 260 270 280 290 300 LEHLHPYSLK KVQSNDNISI LAGAIKCGKT RLIDHVFLMK RKPIIAIDGP AGSGKSTITK 310 320 330 340 350 360 LIAKELNLLY LDTGAMYRAI SWLFKKEKID YAKESELKKI LNNISIIFKS NSISQQDVFI 370 380 390 400 410 420 NNFCVTEEIR SQEISSIVSK ISSIKKVREF LVYEQRKIGQ SGGLVAEGRD IGTTVFPNAE 430 440 450 460 470 480 LKIFLTASID ERAKRRKSEL DLRGTEEIDF NQLRELIRKR DFEDSTRKIS PLKKANDAIE 490 500 510 LLTDGYSINE VVEKIVNIYN LNIPKEIQLE

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CCMP1986 / MED4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX548174 Genomic DNA. Translation: CAE20049.1.
RefSeq	NP_893707.1. NC_005072.1.
3D structure databases
ProteinModelPortal	Q7UZR6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7UZR6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1726235.
GenomeReviews	Gene locus PMM1590 in contig BX548174_GR.
KEGG	pmm:PMM1590.
NMPDR	fig|59919.1.peg.1586.
PATRIC	23034364. VBIProMar68066_1831.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
OMA	LGEKDWQ.
PhylomeDB	Q7UZR6.
ProtClustDB	PRK13477.
Enzyme and pathway databases
BioCyc	PMAR167540:PMM1590-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: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_PROMP

Accession

Primary (citable) accession number: Q7UZR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program