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A5WHC9 (PANC_PSYWF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:PsycPRwf_2130
OrganismPsychrobacter sp. (strain PRwf-1) [Complete proteome] [HAMAP]
Taxonomic identifier349106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceInferred 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-Rule MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000076861

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1541Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5WHC9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 3C9D1E83E37FBB2F

FASTA28631,674
        10         20         30         40         50         60 
MTITFNAIQD LQQALHPLRT DKKIALVPTM GNLHDGHISL VKLAQEHADV VVVSIFVNPT 

        70         80         90        100        110        120 
QFGVGEDLDS YPRTLEADTQ KLTEAGVDYI FAPSVEEMYP VMPPPTQVLA GAISQYLCGK 

       130        140        150        160        170        180 
SRPTHFDGVG IVVTKLFNIV QPNVAVFGKK DYQQLAIIKQ LVRDLSYNIE IIGAPLVRAV 

       190        200        210        220        230        240 
DGLALSSRNQ YLTETERQIA PMLNQHLSKL AQKLKNTPIA NNQQLQALIE DTIAQINNAG 

       250        260        270        280 
FRVDYLEVSN QDLSKITDFY GQKQWVIAVA AWLGKARLLD NQEVNG 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter sp. PRwf-1."
US DOE Joint Genome Institute
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PRwf-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000713 Genomic DNA. Translation: ABQ95070.1.
RefSeqYP_001281020.1. NC_009524.1.

3D structure databases

ProteinModelPortalA5WHC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349106.PsycPRwf_2130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ95070; ABQ95070; PsycPRwf_2130.
GeneID5206503.
KEGGprw:PsycPRwf_2130.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAIRELRAW.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycPPRW349106:GHZF-2180-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_PSYWF
AccessionPrimary (citable) accession number: A5WHC9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways