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Reviewed, UniProtKB/Swiss-Prot Q89ZR8 (PANC_BACTN)

Last modified November 3, 2009. Version 41. 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: BT_4308
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [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_0000305400

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
Q89ZR8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F2D107024D54785E

FASTA28231,564
        10         20         30         40         50         60 
MKVIHTIKDL QAELTALRAQ GKKVGLVPTM GALHAGHASL VKRSVSENGV TVVSVFVNPT 

        70         80         90        100        110        120 
QFNDKNDLAK YPRTLDADCR LLEDCGAAFA FAPSVEEMYP QPDTREFSYA PLDTVMEGAF 

       130        140        150        160        170        180 
RPGHFNGVCQ IVSKLFDAVQ PDRAYFGEKD FQQLAIIREM VRQMDYKLEI VGCPIVREED 

       190        200        210        220        230        240 
GLALSSRNKR LSARERENAL NISQTLFKSR TFAASHTVSE TQKMVEEAIE DAPGLRLEYF 

       250        260        270        280 
EIVDGNTLQK VSSWEDSLYV VGCITVFCGE VRLIDNIKYK EI 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO79413.1.
RefSeqNP_813219.1.

3D structure databases

HSSPHSSP built from PDB template 1N2E based on UniProtKB O06280.
ModBaseSearch...

Genome annotation databases

GeneID1073735.
GenomeReviewsGene locus BT_4308 in contig AE015928_GR.
KEGGbth:BT_4308.
NMPDRfig|226186.1.peg.4306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ89ZR8.
OMAVADFNIP.

Enzyme and pathway databases

BioCycBTHE226186:BT_4308-MON.
BRENDA6.3.2.1. 21018.

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_BACTN
AccessionPrimary (citable) accession number: Q89ZR8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 41 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