Reviewed, UniProtKB/Swiss-Prot Q110U9 (PANCY_TRIEI)

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:	Tery_2799

Organism

Trichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]

Taxonomic identifier

203124 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriales › Trichodesmium

Protein attributes

Sequence length	528 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; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: 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 – 528	528	Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349		PRO_0000333303
Regions
	Nucleotide binding	34 – 41	8	ATP By similarity
	Nucleotide binding	160 – 163	4	ATP By similarity
	Nucleotide binding	197 – 200	4	ATP By similarity
	Region	1 – 293	293	Pantoate--beta-alanine ligase HAMAP MF_01349
	Region	294 – 528	235	Cytidylate kinase HAMAP MF_01349
Sites
	Active site	41	1	Proton donor By similarity
	Binding site	65	1	Beta-alanine By similarity
	Binding site	65	1	Pantoate By similarity
	Binding site	166	1	Pantoate By similarity
	Binding site	189	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q110U9-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: EC536758F6078812	FASTA	528	58,427
	10 20 30 40 50 60 MRLFTTIAGL NCYLNLLRNE QKKSPDTIGL VPTMGALHKG HLSLIKRARE ENTITVVSIF 70 80 90 100 110 120 INPLQFAPRE DFKEYPRQLE IDKEFCEKEG VDVIFAPTPE TMGMKNALST DAQDSTTTVV 130 140 150 160 170 180 SPSHMTSIMC GVSRPNFFQG VATIVTKLLN IVKPNNAYFG QKDAQQLAII KQLVKDLSLP 190 200 210 220 230 240 VNIVYCPIIR EASGLAISSR NQYLTPEQKE QASMLYASLC YGRKIFLENQ DTPNILETVE 250 260 270 280 290 300 NAVKEKLASQ PVLKLEYLEI VDPETLKPLE NIQNIGLLAI AAYIGSCRLI DNILLRNRKP 310 320 330 340 350 360 IIAIDGPAGA GKSTVTKLVG QSLGLLYLDT GAMYRAVTWM VLQSGVPVTD QAQVAELVSQ 370 380 390 400 410 420 CQISFNSPEN NHVVINGQDV TVAIRSREVT NNVSIVAAQP TVRYFMVKQQ QQFGAKGGIV 430 440 450 460 470 480 AEGRDIGSHV FPNAELKIFL TASLKERSRR RLVELKQKGQ TNISLEEVEK EIICRDQKDT 490 500 510 520 NRKISPLRKS SDAVEISTDG LSIGEVTQKI VDIFKTTCYG KSSVNNII

References

[1]

"Complete sequence of Trichodesmium erythraeum IMS101." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000393 Genomic DNA. Translation: ABG51975.1.
RefSeq	YP_722448.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4245333.
GenomeReviews	Gene locus Tery_2799 in contig CP000393_GR.
KEGG	ter:Tery_2799.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q110U9.
OMA	Q110U9. LGEKDWQ.
Enzyme and pathway databases
BioCyc	TERY203124:TERY_2799-MON.
Family and domain databases
HAMAP	MF_01349. [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]
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. TIGR00125. cyt_tran_rel. 1 hit. TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANCY_TRIEI

Accession

Primary (citable) accession number: Q110U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	August 22, 2006
Last modified:	June 16, 2009
This is version 22 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)