Reviewed, UniProtKB/Swiss-Prot Q7V583 (PANCY_PROMM)

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:	PMT_1689

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	505 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; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: 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 – 505	505	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000239791
Regions
	Nucleotide binding	281 – 289	9	ATP By similarity
	Region	1 – 268	268	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	269 – 505	237	Cytidylate kinase HAMAP MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q7V583-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: BFE647766ADDC12F	FASTA	505	55,363
	10 20 30 40 50 60 MHQWRKHQQS SVHFVPTMGA LHRGHGQLIK SVHGFGRLQP AAVLVSVFVN PLQFGPAEDF 70 80 90 100 110 120 DSYPRDLEAD CELASRSGAS ALWAPSVDQV FPGGASSHFR IQVPSHLQAH LCGASRPGHF 130 140 150 160 170 180 DGVVTVVARL LALVRPEVLV LGEKDWQQLV ILRHLVAQLG LPVRVHGIAT VRDDDGLACS 190 200 210 220 230 240 SRNRYLMTQQ RQQALALPQL LARAARESQD GRAVDLAGLR CAWEQLGLEV EYVEKVDAFN 250 260 270 280 290 300 LQPLHAGRKL CLLAAAVRCG ETRLIDHTFL MSRQPIVAID GPAGAGKSTV TRAFAERLGL 310 320 330 340 350 360 LYLDTGAMYR AVTWLTQQHD VDPHDPVAVK TILENLELEL EPSQSGAQTV RINGHDVTEA 370 380 390 400 410 420 IRSPEVTSSV SVVAAHGCVR KALTAQQQRM GVRGGLVAEG RDIGTAVFPD AELKVFLTAS 430 440 450 460 470 480 PAERARRRAL DLDNRGFPVP DLAELETQIE ERDRMDSTRE VAPLRQAEDA TELISDGMTI 490 500 EEVIETLIDL FRVQVPEEVW PTAGR

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX548175 Genomic DNA. Translation: CAE21864.1.
RefSeq	NP_895516.1.
3D structure databases
HSSP	HSSP built from PDB template 1KDO based on UniProtKB P23863.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V583.
Genome annotation databases
GeneID	1728207.
GenomeReviews	Gene locus PMT_1689 in contig BX548175_GR.
KEGG	pmt:PMT1689.
NMPDR	fig|74547.1.peg.1683.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7V583.
OMA	LGEKDWQ.
Enzyme and pathway databases
BioCyc	PMAR74547:PMT1689-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_PROMM

Accession

Primary (citable) accession number: Q7V583

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 35 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)