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Reviewed, UniProtKB/Swiss-Prot Q2YPI2 (PANC_BRUA2)

Last modified November 24, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BAB1_0359
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm Potential.

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: 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 – 293293Pantothenate synthetase HAMAP MF_00158
PRO_0000305411

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YPI2-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: AB9C37F693BD5316

FASTA29332,506
        10         20         30         40         50         60 
MQIIHTIEEL RQALAPARQQ GKKIGFVPTM GYLHKGHLEL VRRARVENDV TLVSIFVNPL 

        70         80         90        100        110        120 
QFGANEDLGR YPRDLERDAG LLHDAQVDYL FAPTVSDMYP RPMQTVVDVP PLGNQIEGEA 

       130        140        150        160        170        180 
RPGHFAGVAT VVSKLFNIVG PDAAYFGEKD FQQLVIIRRM VDDMAIPVRI VGVETVREDD 

       190        200        210        220        230        240 
GLACSSRNVY LTPEQRRAAI IVPQALDEAD RLYRSGMDDP DALEAAIRTF IGRQPLAVPE 

       250        260        270        280        290 
VIAIRDPETL ERLPALQGRP ILVALFVRVG ATRLLDNRVI GHAAPQITQE RAA 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM040264 Genomic DNA. Translation: CAJ10315.1.
RefSeqYP_413826.1.

3D structure databases

HSSPHSSP built from PDB template 2A84 based on UniProtKB P0A5R0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2YPI2.

Genome annotation databases

GeneID3787130.
GenomeReviewsGene locus BAB1_0359 in contig AM040264_GR.
KEGGbmf:BAB1_0359.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2YPI2.
OMAMPIQIIG

Enzyme and pathway databases

BioCycBMEL359391:BAB1_0359-MON.

Family and domain databases

HAMAPMF_00158.
[Tree]
InterProIPR004821. Cyt_trans_rel.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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_BRUA2
AccessionPrimary (citable) accession number: Q2YPI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 20, 2005
Last modified: November 24, 2009
This is version 25 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

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