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:	CYB_2425

From

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)

[TaxID: 321332]

[HAMAP proteome]

Taxonomy

Bacteria; Cyanobacteria; Chroococcales; Synechococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ismej.2007.46; PubMed=18059494 [NCBI, ExPASy, EBI, Israel, Japan]
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses.";
ISME J. 1:703-713(2007).

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

CP000240; ABD03359.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_478622.1; -.

3D structure databases

ModBase

Q2JJ30.

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

IPR004821; Cyt_trans_rel.
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.
TIGR00125; cyt_tran_rel; 1.
TIGR00018; panC; 1.

ProtoNet

Q2JJ30.

Genome annotation databases

GeneID

3901394; -.

GenomeReviews

CP000240_GR; CYB_2425.

KEGG

cyb:CYB_2425; -.

TIGR

CYB_2425; -.

Phylogenomic databases

HOGENOM

Q2JJ30; -.

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`	`1 542`	`542`	`Bifunctional pantoate ligase/cytidylate kinase.`	`PRO_0000239796`
`NP_BIND`	`317 325`	`9`	`ATP (By similarity).`
`REGION`	`1 280`	`280`	`Pantoate--beta-alanine ligase.`
`REGION`	`281 542`	`262`	`Cytidylate kinase.`

Sequence information

Length: 542 AA [This is the length of the unprocessed precursor]

Molecular weight: 59857 Da [This is the MW of the unprocessed precursor]

CRC64: BE1BF4BB355F078A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHWLRTVAAL REQVADWRGS TVGLVPTMGS LHEGHLSLIR RCRQECDHTV VSIFVNPLQF 

        70         80         90        100        110        120 
GPNEDWDRYP RDEEGDRALC EAAGVDVVFA PDPQEMGADP ATGSDRTWVM PPESLLQTLC 

       130        140        150        160        170        180 
APHRPGHFRG VATIVLQLLN LVQPQRAYFG QKDAQQLAII QRLVRDLQIP TTIVPCSTVR 

       190        200        210        220        230        240 
EADGLACSSR NRYLSAAERQ VAAGLYRALR RGYDHWQAGD PSAEGILAAA RAELEHTPEL 

       250        260        270        280        290        300 
QLQYLELVDP QTLQPLPRVE DKGLLAIAAY VGQTRLIDNL LLSPEQGDPL PERVQHAAPP 

       310        320        330        340        350        360 
SSGTTSPPRR PLIAIDGPAG AGKSTVARAV AAQLQLLYLD TGAMYRAITW LALQRGIPLD 

       370        380        390        400        410        420 
DAEQLTQLAA QTQLTLQSGT SSTEPTRIWA DGEEITQAIR SPEVTRWVSH VAAVPGVRQE 

       430        440        450        460        470        480 
LVKRQRSIGR DGGAVLEGRD IGTHVFPDAE LKVFLTASVG ERAQRRQHQL QAQGQMVPLE 

       490        500        510        520        530        540 
ELKAQIEQRD RRDSERLISP LRPAPDAILI DTDHLSQSEV QDKIVMLYRQ LLERSGPARL 


DQ

Q2JJ30 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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