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Q5P9T3 (PANC_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:AM1089
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

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.

Sequence caution

The sequence AAV86947.1 differs from that shown. Reason: Erroneous initiation.

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_0000305391

Regions

Nucleotide binding28 – 358ATP By similarity
Nucleotide binding145 – 1484ATP By similarity
Nucleotide binding182 – 1854ATP By similarity

Sites

Active site351Proton donor By similarity
Binding site591Beta-alanine By similarity
Binding site591Pantoate By similarity
Binding site1741ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P9T3 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 29ADC2883893FD5E

FASTA27731,057
        10         20         30         40         50         60 
MEIVRDVESV RAVLRPFTNR KIGLVPTMGA LHSGHLSLVH EMKKHADVVI VSIFVNPLQF 

        70         80         90        100        110        120 
SPGEDYEKYP RCEEVDCEKC ASAGVDVVYI PSAEGMYPDG FSTSVDIGPM ARELCGASRQ 

       130        140        150        160        170        180 
NFINGIMVVL IKLVMQTNAH CMILGEKDYQ MLHLTRQLFR DLNIGVDVLQ GNTVRSAEGL 

       190        200        210        220        230        240 
ALSSRHQYLS SAEITKANFL YGFLLEVGQQ LSDDPHGQQE IIARGKLRLE QEGFEVDYLE 

       250        260        270 
VRDNNTLEHM QTFRKPARVF LAVYLGNCRL IDNVLLA 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86947.1. Different initiation.
RefSeqYP_154202.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5P9T3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM1089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86947; AAV86947; AM1089.
GeneID3171235.
KEGGama:AM1089.
PATRIC20948069. VBIAnaMar46146_0947.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

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_ANAMM
AccessionPrimary (citable) accession number: Q5P9T3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 58 of the entry and version 2 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