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Reviewed, UniProtKB/Swiss-Prot A0LRC5 (PANC_ACIC1)

Last modified February 9, 2010. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Acel_0211
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length303 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 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 Potential 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.

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Pantothenate synthetase HAMAP MF_00158
PRO_0000305382

Regions

Nucleotide binding48 – 558ATP By similarity
Nucleotide binding165 – 1684ATP By similarity
Nucleotide binding202 – 2054ATP By similarity

Sites

Active site551Proton donor By similarity
Binding site791Beta-alanine By similarity
Binding site791Pantoate By similarity
Binding site1711Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LRC5-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 4963B0D9CD3BC119

FASTA30332,219
        10         20         30         40         50         60 
MIATGHGGAE RRTTAGDGTA RPVVARTIGE LRAARAALTG PVAFVPTMGA LHDGHRSLLR 

        70         80         90        100        110        120 
IARHHGDHVV VSIFVNPLQF GPAEDFDRYP RTLDADLAMC AAEGVDLVFV PPAAEMYPSE 

       130        140        150        160        170        180 
PQVRVSAGPL GERFEGSVRP GHFDGVLTVV AKLFQLVQPD VAVFGRKDAQ QLALVRRMVA 

       190        200        210        220        230        240 
DLNLPVQIIA APTFREPDGL AASSRNRYLT DADRAQARAL PTALTTAAAV AAAGGPPSEM 

       250        260        270        280        290        300 
IEMARKVLAD AAVTLDYVAV VDEATFDEID DAEWSQRGEG LCIAAIRVGG TRLIDNMPMR 


KAD 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK51985.1.
RefSeqYP_871971.1.

3D structure databases

SMRA0LRC5. Positions 23-300.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LRC5.

Genome annotation databases

GeneID4486069.
GenomeReviewsGene locus Acel_0211 in contig CP000481_GR.
KEGGace:Acel_0211.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHBG428839.
OMAEDFGSYP.
PhylomeDBA0LRC5.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR004821. Cyt_trans_rel.
IPR003721. Pantoate_ligase.
[Graphical view]
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_ACIC1
AccessionPrimary (citable) accession number: A0LRC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: February 9, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents