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B4RYN9 (PANC_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:panC1
Ordered Locus Names:MADE_1017490
AND
Name:panC2
Ordered Locus Names:MADE_1018445
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097028

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding149 – 1524ATP By similarity
Nucleotide binding186 – 1894ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1551Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RYN9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: AC943C3604B879E8

FASTA28230,833
        10         20         30         40         50         60 
MKVIDSISTL RQTVNAWRRN GESVGFVPTM GNLHDGHLKL VKKAKAHNDN VVVSIFVNPM 

        70         80         90        100        110        120 
QFGANEDLDA YPRTIEEDKA KLISVGADAV FLPSVAEMYP AGLDAQTFVE VPGISDSHCG 

       130        140        150        160        170        180 
ASRPGHFRGV ATVVTKLFNM VQPDDAFFGE KDFQQLQVIR ALARDLSMAV TIHGVPTERE 

       190        200        210        220        230        240 
ASGLAMSSRN GYLSKEEKAT ASAIYEEMQR VKAGIEGGNI DFSELEDAMV TNLEAKGFKK 

       250        260        270        280 
DYCQVVNAST FKAATANDKE LVLLVAMFMG KTRLIDNLQI TR 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA99622.1.
CP001103 Genomic DNA. Translation: AEA99813.1.
RefSeqYP_004428811.1. NC_011138.3.

3D structure databases

ProteinModelPortalB4RYN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_03551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA99622; AEA99622; MADE_1017490.
AEA99813; AEA99813; MADE_1018445.
GeneID10559035.
KEGGamc:MADE_1018445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
KOK01918.
OMAQPDKAFF.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-3530-MONOMER.
AMAC314275:GHA7-3721-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_ALTMD
AccessionPrimary (citable) accession number: B4RYN9
Secondary accession number(s): F2G683
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 43 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