Reviewed, UniProtKB/Swiss-Prot B0C6S1 (PANCY_ACAM1)

Names and origin

Protein names

Recommended name:
    Bifunctional pantoate ligase/cytidylate kinase
Including the following 2 domains:
    1- Recommended name:
            Pantothenate synthetase
                Short name=PS
              EC=6.3.2.1
        Alternative name(s):
            Pantoate--beta-alanine ligase
            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:	AM1_2620

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. Displays a CMP kinase activity By similarity.
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 – 525	525	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333294
Regions
	Nucleotide binding	44 – 51	8	ATP By similarity
	Nucleotide binding	162 – 165	4	ATP By similarity
	Nucleotide binding	199 – 202	4	ATP By similarity
	Region	1 – 292	292	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	293 – 525	233	Cytidylate kinase HAMAP MF_01349
Sites
	Active site	51	1	Proton donor By similarity
	Binding site	75	1	Beta-alanine By similarity
	Binding site	75	1	Pantoate By similarity
	Binding site	168	1	Pantoate By similarity
	Binding site	191	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0C6S1-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: EE2A7EA486E0C84A	FASTA	525	57,533
	10 20 30 40 50 60 MDNVPIIRTV SGLRHFLRCF PGNLNTGASP SSTVIGQIGL VPTMGALHAG HLSLIQRARQ 70 80 90 100 110 120 ENQCVIVSIF VNPLQFAAHE DLTEYPQTLN QDQALCQEQG VNTIFAPSTD TLLADAPLTQ 130 140 150 160 170 180 VIPPASLTEY LCGPHRPDHF TGVATIVLKL LNIVQPTRAY FGQKDAQQLA IIQRLVQDFN 190 200 210 220 230 240 LDVTIVPCKL IRDATGLALS SRNQYLNAQE AQQATILHHS LQAARHTFQG GSCDRNSVLA 250 260 270 280 290 300 TVAQTLAKGP QVEVEYIDLV DPVTLQPLEQ ITTQGLVAIA ARVGSARLID NMLLDARLPI 310 320 330 340 350 360 LAIDGPAGAG KSTVTRRCAQ AIGLQYLDTG AMYRAVAWLA LDQQVEVSDP FAIADLVEDC 370 380 390 400 410 420 QIELKPHADP QQQPQVWVNH QEVTQAIRTP DVTALVSAVA AQPPVREALV KQQQRLGRQG 430 440 450 460 470 480 GLIAEGRDIG TNVFPDAGLK IFLTASIEER ARRRQQDLKN QNLPPQTQSE LEDLIASRDQ 490 500 510 520 QDSQREFAPL RKAYDAVEIN TDGMTIEQVI TRITTLYQER FPDRA

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000828 Genomic DNA. Translation: ABW27627.1.
RefSeq	YP_001516941.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5681432.
GenomeReviews	Gene locus AM1_2620 in contig CP000828_GR.
KEGG	amr:AM1_2620.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	LGEKDWQ.
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_ACAM1

Accession

Primary (citable) accession number: B0C6S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	November 3, 2009
This is version 12 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)