Reviewed, UniProtKB/Swiss-Prot Q55074 (PANCY_SYNY3)

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
Synonyms:	panC/kcy
Ordered Locus Names:	sll1249

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	513 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.
Sequence caution	The sequence AAA86660.1 differs from that shown. Reason: Frameshift at positions 213, 240, 254 and 258.

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 – 513	513	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000131992
Regions
	Nucleotide binding	296 – 304	9	ATP By similarity
	Region	1 – 283	283	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	284 – 513	230	Cytidylate kinase HAMAP MF_01349

Sequences

	Sequence		Length	Mass (Da)
	Q55074-1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: 5A216A6E718A677B	FASTA	513	55,452
	10 20 30 40 50 60 MVQVFRTIAG LQTYLRQAGR GKTVGLVPTM GSLHAGHGSL LKRAVAEMDL VVLSIFVNPL 70 80 90 100 110 120 QFGPGEDLEK YPRDFDGDRQ WAESLGVAVI FAPTVTDLGI DAKGDQTTVL PPPAMTEVLC 130 140 150 160 170 180 GAHRPGHFQG VATIVTKLFT IVCPDVAYFG AKDAQQLAII RRLVQDLNLT VTIRSCATVR 190 200 210 220 230 240 EESGLAMSSR NQYLSPIEKE QATVLYRSLQ AAQQRYRQGD RQVSALLTAT QDVLDAEPSV 250 260 270 280 290 300 QVQYLQLVEA DTLQPITGTL PDQNPVLMAI AAYVGSTRLI DNLVLNHRLP IIAIDGPAGA 310 320 330 340 350 360 GKSTVTRQVA DGLGLTYLDT GAMYRALAWL ILDQGIAPED EPAVAELTSG AEIELMPRPA 370 380 390 400 410 420 PQLTGVKVNG QDVSDAIRTP AVTQLVSTIA AQGAVRAKLL KLQRKYGDQG GIVAEGRDIG 430 440 450 460 470 480 TQVFPNAELK IFLTASVQER ARRRLKDFEA QGNQAVDLAQ LEADIAHRDH LDSTRAIAPL 490 500 510 QKAVDAVEII TDNLTIAEVV ETIIELYKKY NKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803." So A.K.C., Espie G.S. Plant Mol. Biol. 37:205-215(1998) [PubMed: 9617794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U44896 Genomic DNA. Translation: AAA86660.1. Frameshift. U44896 Genomic DNA. Translation: AAA86661.1. BA000022 Genomic DNA. Translation: BAA18165.1.
PIR	S75604.
RefSeq	NP_441485.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q55074. 1 interaction.
STRING	Q55074.
Genome annotation databases
GeneID	954865.
GenomeReviews	Gene locus sll1249 in contig BA000022_GR.
KEGG	syn:sll1249.
NMPDR	fig|1148.1.peg.1586.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q55074.
OMA	LGEKDWQ.
Enzyme and pathway databases
BioCyc	SSP1148:SLL1249-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_SYNY3

Accession

Primary (citable) accession number: Q55074
Secondary accession number(s): P74087, Q55073

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)