Pantoate--beta-alanine ligase
     (EC 6.3.2.1)
     (Pantothenate synthetase)
     (Pantoate-activating enzyme)
Cytidylate kinase
     (CK)
     (EC 2.7.4.14)
     (Cytidine monophosphate kinase)
     (CMP kinase)

Gene name

	Name:	panC/cmk
	OrderedLocusNames:	PMM1590

From

Prochlorococcus marinus subsp. pastoris (strain CCMP1378 / MED4)

[TaxID: 59919]

[HAMAP proteome]

Taxonomy

Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(2003).

Comments

CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.
CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP.
PATHWAY: Cofactor biosynthesis; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: step 1/1 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the pantothenate synthetase family.
SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX548174; CAE20049.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_893707.1; -.

3D structure databases

HSSP

P23863; 1CKE. [HSSP ENTRY / PDB]

ModBase

Q7UZR6.

Enzyme and pathway databases

BioCyc

PMAR167540:PMM1590-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004127;	Molecular function: cytidylate kinase activity (inferred from electronic annotation from HAMAP).
GO:0004592;	Molecular function: pantoate-beta-alanine ligase activity (inferred from electronic annotation from HAMAP).
GO:0015940;	Biological process: pantothenate biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006220;	Biological process: pyrimidine nucleotide metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01349; -; 1.
PBIL [Tree]

InterPro

IPR003136; Cytidylate_kin.
IPR011994; Cytidylate_kin_d.
IPR003721; Pantoate_ligase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

PANTHER

PTHR21299:SF1; Pantoate_ligase; 1.

Pfam

PF02224; Cytidylate_kin; 1.
PF02569; Pantoate_ligase; 1.
Pfam graphical view of domain structure.

ProDom

PD000657; Adenylate_kin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00017; cmk; 1.
TIGR00018; panC; 1.

Genome annotation databases

GeneID

1726235; -.

GenomeReviews

BX548174_GR; PMM1590.

KEGG

pmm:PMM1590; -.

NMPDR

fig|59919.1.peg.1586; -.

Phylogenomic databases

HOGENOM

Q7UZR6; -.

Genome annotation databases

CMR

Q7UZR6; PMM1590.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Kinase; Ligase; Multifunctional enzyme; Nucleotide-binding; Pantothenate biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 510`	`510`	`Bifunctional pantoate ligase/cytidylate kinase.`	`PRO_0000239792`
`NP_BIND`	`289 297`	`9`	`ATP (By similarity).`
`REGION`	`1 276`	`276`	`Pantoate--beta-alanine ligase.`
`REGION`	`277 510`	`234`	`Cytidylate kinase.`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 58295 Da [This is the MW of the unprocessed precursor]

CRC64: 315DC94E014CBDF8 [This is a checksum on the sequence]

        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

Q7UZR6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools