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Q5SHF5 (PANC_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:TTHA1775
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 MF_00158

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 Probable. Ref.2

Subcellular location

Cytoplasm Potential HAMAP MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158

PDB 1UFV apparently has a Val-49-Ala mutation. HAMAP MF_00158

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Pantothenate synthetase HAMAP MF_00158
PRO_0000128283

Regions

Nucleotide binding25 – 328ATP By similarity
Nucleotide binding143 – 1464ATP By similarity
Nucleotide binding180 – 1834ATP By similarity

Sites

Active site321Proton donor By similarity
Binding site561Beta-alanine By similarity
Binding site561Pantoate By similarity
Binding site1491Pantoate By similarity
Binding site1721ATP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1 ................................................. 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHF5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 975B6B82D162AE40

FASTA27630,695
        10         20         30         40         50         60 
MRTVSTVAEL RAALPREGVG FVPTMGYLHR GHLALVERAR RENPFVVVSV FVNPLQFGPG 

        70         80         90        100        110        120 
EDYHRYPRDL ERDRALLQEA GVDLLFAPGV EEMYPEGFAT RVQVEGPLTA LWEGAVRPGH 

       130        140        150        160        170        180 
FQGVATVVAR LFLLVQPQRA YFGEKDYQQL LVVRRMVRDL GFPVEVVGVP TVREEDGLAL 

       190        200        210        220        230        240 
SSRNVYLSPE TRKKAPVLYR ALLAMREVAG QGGSVAEALR AGEEALRAVP EFRKDYLAIV 

       250        260        270 
HPETLLPLSD WVAGARGIVA GRFPEARLID NLEVYP

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Crystal structure of pantothenate synthetase from Thermus thermophilus HB8."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2003) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008226 Genomic DNA. Translation: BAD71598.1.
RefSeqYP_145041.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFVX-ray2.05A/B1-276[»]
1V8FX-ray1.90A/B1-276[»]
ProteinModelPortalQ5SHF5.
SMRQ5SHF5. Positions 1-276.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5SHF5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3169469.
GenomeReviewsGene locus TTHA1775 in contig AP008226_GR.
KEGGttj:TTHA1775.
PATRIC23958511. VBITheThe93045_1745.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHBG428839.
OMALNMPIQI.
PhylomeDBQ5SHF5.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycTTHE300852:TTHA1775-MONOMER.

Family and domain databases

HAMAPMF_00158. PanC.
[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.
KOK01918.
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_THET8
AccessionPrimary (citable) accession number: Q5SHF5
Secondary accession number(s): P83701
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 21, 2004
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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