Reviewed, UniProtKB/Swiss-Prot Q31P38 (PANCY_SYNE7)

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:	Synpcc7942_1151

Organism

Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]

Taxonomic identifier

1140 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	527 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 – 527	527	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000239798
Regions
	Nucleotide binding	290 – 298	9	ATP By similarity
	Region	1 – 277	277	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	278 – 527	250	Cytidylate kinase HAMAP MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q31P38-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 1D7DAFE30F0944E0	FASTA	527	57,098
	10 20 30 40 50 60 MRQLISPEAL RAFRQSVQGS VGFVPTMGAL HAGHRSLIER SRQQDDVVIV SIFVNPRQFG 70 80 90 100 110 120 PQEDLSRYPQ TLDADLALCE AAGVDAVFCP TAEALYPRPS DRSTGVQPPA ELIQSLCGRQ 130 140 150 160 170 180 RPGHFQGVAT VVLKLLQLVQ PQRAYFGEKD AQQLRVIQRL VEDFNLPIAI VPCPTVREPD 190 200 210 220 230 240 GLALSSRNRY LTFEERSQAS GLYRALRAAA ECFQAGSRDS QELVAAATAV LATTPAVQLE 250 260 270 280 290 300 YCDCVDADSL QPLTQIPDRA LLAIAARVGT ARLIDNLTLQ GRRPIIAIDG PAGAGKSTVT 310 320 330 340 350 360 KRLAQQLGLL YLDTGAMYRA VTWLVQQQGI DPQDPIVLAE LLAQADLQLR SQPAADGSEQ 370 380 390 400 410 420 LQVLIQGNDV TAAIRTPTVT AQVSAIAALP LVRQFLVEQQ RQLGQRGGLV AEGRDIGTHV 430 440 450 460 470 480 FPDAELKIFL TATNAERARR RALDLEAQGL TVDLAQLEAE IRDRDRQDSE RAIAPLCKAE 490 500 510 520 DAVEVLTDGL SIEAVTDQII RLYRDRGLGD SSPQATPGQT PSPLSLG

References

[1]

"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000100 Genomic DNA. Translation: ABB57181.1.
RefSeq	YP_400168.1.
3D structure databases
SMR	Q31P38. Positions 1-280, 217-309, 283-506.
ModBase	Search...
Protein-protein interaction databases
STRING	Q31P38.
Genome annotation databases
GeneID	3775101.
GenomeReviews	Gene locus Synpcc7942_1151 in contig CP000100_GR.
KEGG	syf:Synpcc7942_1151.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
Enzyme and pathway databases
BioCyc	SELO1140:SYNPCC7942_1151-MONOMER.
Family and domain databases
HAMAP	MF_01349. PanCY. [Tree]
InterPro	IPR004821. Cyt_trans_rel. 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. TIGR00125. cyt_tran_rel. 1 hit. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_SYNE7

Accession

Primary (citable) accession number: Q31P38

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	December 6, 2005
Last modified:	February 9, 2010
This is version 26 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)