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C1D7E9 (PANC_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 36. 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:LHK_01399
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeLaribacter

Protein attributes

Sequence length277 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 – 277277Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000123416

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding144 – 1474ATP By similarity
Nucleotide binding181 – 1844ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1501Pantoate By similarity
Binding site1731ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
C1D7E9 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: DB9AE0FAF1E14E25

FASTA27731,324
        10         20         30         40         50         60 
MDIIRTIEEM RSWRQKAGRV ALVPTMGNLH EGHLALVREA KKQAERVVVS IFVNRLQFGQ 

        70         80         90        100        110        120 
GEDFDSYPRT FEADRDKLAA AGVDALFLPD ERELYPRIRQ DFNVEPPHIQ DELCGAFRPG 

       130        140        150        160        170        180 
HFRGVATVVT KLFNIVQPDA ACFGKKDFQQ LHIIQAMVAD LNQPVKVVPV DIGRAADGLA 

       190        200        210        220        230        240 
LSSRNGYLSA GEREEAPRLF RELSRIRENL IDGENDYASL EQDARATLEQ HGWRVDYVEI 

       250        260        270 
RQADTLELAH AGEKRLVVLA AARIGKTRLI DNVEIFR 

« Hide

References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO74389.1.
RefSeqYP_002795398.1. NC_012559.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557598.LHK_01399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO74389; ACO74389; LHK_01399.
GeneID7757018.
KEGGlhk:LHK_01399.
PATRIC22299791. VBILarHon49832_1290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAIHTIREL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycLHON557598:GHO5-1430-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_LARHH
AccessionPrimary (citable) accession number: C1D7E9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 36 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