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Protein

Pantothenate synthetase

Gene

panC

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.UniRule annotation

Catalytic activityi

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.UniRule annotation

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Pantothenate synthetase (panC)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei32Proton donorUniRule annotation1
Binding sitei56Beta-alanineUniRule annotation1
Binding sitei56PantoateUniRule annotation1
Binding sitei149PantoateUniRule annotation1
Binding sitei172ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi25 – 32ATPUniRule annotation8
Nucleotide bindingi143 – 146ATPUniRule annotation4
Nucleotide bindingi180 – 183ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
Short name:
PSUniRule annotation
Alternative name(s):
Pantoate--beta-alanine ligaseUniRule annotation
Pantoate-activating enzymeUniRule annotation
Gene namesi
Name:panCUniRule annotation
Ordered Locus Names:TTHA1775
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001282831 – 276Pantothenate synthetaseAdd BLAST276

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA1775.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi7 – 13Combined sources7
Beta strandi19 – 24Combined sources6
Helixi30 – 42Combined sources13
Beta strandi44 – 50Combined sources7
Helixi54 – 56Combined sources3
Turni63 – 65Combined sources3
Helixi70 – 79Combined sources10
Beta strandi83 – 86Combined sources4
Helixi90 – 93Combined sources4
Beta strandi100 – 104Combined sources5
Helixi107 – 110Combined sources4
Helixi113 – 116Combined sources4
Helixi120 – 135Combined sources16
Beta strandi138 – 143Combined sources6
Helixi144 – 146Combined sources3
Helixi147 – 160Combined sources14
Beta strandi165 – 169Combined sources5
Helixi182 – 186Combined sources5
Helixi189 – 194Combined sources6
Helixi197 – 210Combined sources14
Helixi215 – 226Combined sources12
Beta strandi233 – 240Combined sources8
Turni242 – 244Combined sources3
Beta strandi256 – 263Combined sources8
Beta strandi266 – 273Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFVX-ray2.05A/B1-276[»]
1V8FX-ray1.90A/B1-276[»]
ProteinModelPortaliQ5SHF5.
SMRiQ5SHF5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHF5.

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IAA. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175516.
KOiK01918.
OMAiRSVDKLC.
PhylomeDBiQ5SHF5.

Family and domain databases

CDDicd00560. PanC. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SHF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTVSTVAEL RAALPREGVG FVPTMGYLHR GHLALVERAR RENPFVVVSV
60 70 80 90 100
FVNPLQFGPG EDYHRYPRDL ERDRALLQEA GVDLLFAPGV EEMYPEGFAT
110 120 130 140 150
RVQVEGPLTA LWEGAVRPGH FQGVATVVAR LFLLVQPQRA YFGEKDYQQL
160 170 180 190 200
LVVRRMVRDL GFPVEVVGVP TVREEDGLAL SSRNVYLSPE TRKKAPVLYR
210 220 230 240 250
ALLAMREVAG QGGSVAEALR AGEEALRAVP EFRKDYLAIV HPETLLPLSD
260 270
WVAGARGIVA GRFPEARLID NLEVYP
Length:276
Mass (Da):30,695
Last modified:December 21, 2004 - v1
Checksum:i975B6B82D162AE40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71598.1.
RefSeqiWP_011173797.1. NC_006461.1.
YP_145041.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71598; BAD71598; BAD71598.
GeneIDi3169469.
KEGGittj:TTHA1775.
PATRICi23958511. VBITheThe93045_1745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71598.1.
RefSeqiWP_011173797.1. NC_006461.1.
YP_145041.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFVX-ray2.05A/B1-276[»]
1V8FX-ray1.90A/B1-276[»]
ProteinModelPortaliQ5SHF5.
SMRiQ5SHF5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71598; BAD71598; BAD71598.
GeneIDi3169469.
KEGGittj:TTHA1775.
PATRICi23958511. VBITheThe93045_1745.

Phylogenomic databases

eggNOGiENOG4108IAA. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175516.
KOiK01918.
OMAiRSVDKLC.
PhylomeDBiQ5SHF5.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.

Miscellaneous databases

EvolutionaryTraceiQ5SHF5.

Family and domain databases

CDDicd00560. PanC. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPANC_THET8
AccessioniPrimary (citable) accession number: Q5SHF5
Secondary accession number(s): P83701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism.UniRule annotation
PDB 1UFV apparently has a Val-49-Ala mutation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.