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A1S3M6 (PANC_SHEAM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Sama_0775
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length281 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 – 281281Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305544

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
Binding site1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1S3M6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6FC79042913E72B6

FASTA28130,227
        10         20         30         40         50         60 
MYTTAVIDEI RQQVRQWRAS GETVAFVPTM GNLHAGHITL IKEAKQRADH VVASIFVNPM 

        70         80         90        100        110        120 
QFGKNEDLDA YPRTLAEDQA ALTAAGCELL FTPTPDIIYP KGLDAQTFVE VPGISDELCG 

       130        140        150        160        170        180 
ASRPGHFRGV ATIVLKLFNI VQPDVALFGR KDYQQLLVIR TMVEDLSLPL EIVGVETVRE 

       190        200        210        220        230        240 
ASGLAMSSRN GYLTADEKAR AAALKAALDA LAMQIGAGTA IDAAITEANA ALVTAGFRPD 

       250        260        270        280 
YLEVRSATTL ALPTDADKEL VVLAAAYLGK ARLIDNLVFS R 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABL98982.1.
RefSeqYP_926652.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S3M6.
SMRA1S3M6. Positions 1-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326297.Sama_0775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL98982; ABL98982; Sama_0775.
GeneID4603027.
KEGGsaz:Sama_0775.
PATRIC23450145. VBISheAma74963_0806.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycSAMA326297:GH0T-805-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_SHEAM
AccessionPrimary (citable) accession number: A1S3M6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 49 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