C1D1A2 (C1D1A2_DEIDV) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Pantothenate synthetase HAMAP MF_00158
Short name=PS HAMAP MF_00158
EC=6.3.2.1 HAMAP MF_00158

Alternative name(s):
Pantoate--beta-alanine ligase HAMAP MF_00158
Pantoate-activating enzyme HAMAP MF_00158

Gene names

Name:	panC HAMAP MF_00158 EMBL ACO45626.2
Ordered Locus Names:	Deide_07640 EMBL ACO45626.2

Organism

Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]

Taxonomic identifier

546414 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
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. HAMAP MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer By similarity. HAMAP MF_00158
Subcellular location	Cytoplasm By similarity HAMAP MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158
Sequence similarities	Belongs to the pantothenate synthetase family. HAMAP MF_00158

Ontologies

Keywords
Biological process	Pantothenate biosynthesis HAMAP MF_00158
Cellular component	Cytoplasm HAMAP MF_00158
Ligand	ATP-binding HAMAP MF_00158 Nucleotide-binding
Molecular function	Ligase HAMAP MF_00158 EMBL ACO45626.2
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic 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: UniProtKB-KW 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
Regions
	Nucleotide binding	32 – 39	8	ATP By similarity HAMAP MF_00158
	Nucleotide binding	151 – 154	4	ATP By similarity HAMAP MF_00158
	Nucleotide binding	188 – 191	4	ATP By similarity HAMAP MF_00158
Sites
	Active site	39	1	Proton donor By similarity HAMAP MF_00158
	Binding site	65	1	Beta-alanine By similarity HAMAP MF_00158
	Binding site	65	1	Pantoate By similarity HAMAP MF_00158
	Binding site	157	1	Pantoate By similarity HAMAP MF_00158
	Binding site	180	1	ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00158

Sequences

	Sequence		Length	Mass (Da)
	C1D1A2 [UniParc]. Last modified March 8, 2011. Version 2. Checksum: 10C93D8BF98DA4A5	FASTA	295	31,820
	10 20 30 40 50 60 MGAIKTPILI TSTEELRTAL TGAGEIGFVP TMGYLHEGHA TLIRRARQDH PGGRVVVSVF 70 80 90 100 110 120 INPMQFGPSE DLSRYPRNLE GDLQVAGQAG ADIVFHPNAA QMYPEGFSTR VSVSGVSEPL 130 140 150 160 170 180 DGAARPGHFT GVTTVVLKLL NMVRPDRAYF GEKDWQQLAV VRRMVTDLNV PVQVVGVPTV 190 200 210 220 230 240 RDPSGLALSS RNSYLSDEQK ARAAVLARAL RAVQAAFAAG ERHTQALQQA GLDILAADSE 250 260 270 280 290 VTLDYLSVVN SHLQETELVS PDPLNRVLVA ARMFGVRLID NLPLDQGPDD IGRNV

References

[1]

"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti." de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J. PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001114 Genomic DNA. Translation: ACO45626.2.
RefSeq	YP_002785380.2. NC_012526.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	C1D1A2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7738732.
GenomeReviews	Gene locus Deide_07640 in contig CP001114_GR.
KEGG	ddr:Deide_07640.
PATRIC	21615162. VBIDeiDes121019_0865.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00158. PanC. [Tree]
InterPro	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.
KO	K01918.
PANTHER	PTHR21299:SF1. Pantoate_ligase. 1 hit.
Pfam	PF02569. Pantoate_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00018. PanC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

C1D1A2_DEIDV

Accession

Primary (citable) accession number: C1D1A2

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	March 8, 2011
Last modified:	January 25, 2012
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)