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Reviewed, UniProtKB/Swiss-Prot Q64XM3 (PANC_BACFR)

Last modified November 3, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: BF1003
OrganismBacteroides fragilis [Complete proteome] [HAMAP]
Taxonomic identifier817 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP MF_00158
PRO_0000305398

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
Q64XM3-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 07E01A9DBB647E25

FASTA28231,559
        10         20         30         40         50         60 
MKVIHTIKDL QAELSVLKAQ GKKVGLVPTM GALHAGHASL VKRSVNENEV TVVSVFVNPT 

        70         80         90        100        110        120 
QFNDKNDLVK YPRTLDADCK LLEACGATYA FAPSVEEMYP EPDTRQFSYA PLDTVMEGAF 

       130        140        150        160        170        180 
RPGHFNGVCQ IVSKLFEAVK PHRAYFGEKD FQQLAIIREM VRQMQFDLEI VGCPIVREED 

       190        200        210        220        230        240 
GLALSSRNAR LSAEERENAL KISQTLFKSR TFAATHTVSE TLKFVEDAIT AVPGLRLEYF 

       250        260        270        280 
EIVDGNTLQK VDNWNQTSYV VGCITVFCGD VRLIDNIKYK ES 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

AP006841 Genomic DNA. Translation: BAD47753.1.
RefSeqYP_098287.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3081884.
GenomeReviewsGene locus BF1003 in contig AP006841_GR.
KEGGbfr:BF1003.
NMPDRfig|295405.3.peg.1066.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ64XM3.
OMASRNVYLN.

Enzyme and pathway databases

BioCycBFRA295405:BF1003-MON.
BRENDA6.3.2.1. 868.

Family and domain databases

HAMAPMF_00158.
[Tree]
InterProIPR003721. 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]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_BACFR
AccessionPrimary (citable) accession number: Q64XM3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 30 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

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