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Protein

Pantothenate synthetase

Gene

panC

Organism
Staphylococcus aureus (strain NCTC 8325)
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 sitei38Proton donorUniRule annotation1
Binding sitei62Beta-alanineUniRule annotation1
Binding sitei62PantoateUniRule annotation1
Binding sitei154PantoateUniRule annotation1
Binding sitei177ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 38ATPUniRule annotation8
Nucleotide bindingi148 – 151ATPUniRule annotation4
Nucleotide bindingi185 – 188ATPUniRule 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

BRENDAi6.3.2.1. 3352.
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:SAOUHSC_02918
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 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_00003055601 – 283Pantothenate synthetaseAdd BLAST283

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi93061.SAOUHSC_02918.

Structurei

Secondary structure

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi8 – 20Combined sources13
Beta strandi25 – 30Combined sources6
Helixi36 – 46Combined sources11
Beta strandi49 – 56Combined sources8
Helixi60 – 62Combined sources3
Turni69 – 71Combined sources3
Helixi76 – 86Combined sources11
Beta strandi89 – 92Combined sources4
Helixi96 – 99Combined sources4
Beta strandi105 – 110Combined sources6
Helixi112 – 114Combined sources3
Helixi118 – 121Combined sources4
Helixi125 – 140Combined sources16
Beta strandi143 – 148Combined sources6
Helixi149 – 151Combined sources3
Helixi152 – 164Combined sources13
Beta strandi170 – 174Combined sources5
Helixi187 – 191Combined sources5
Helixi194 – 199Combined sources6
Helixi202 – 215Combined sources14
Helixi221 – 235Combined sources15
Beta strandi238 – 247Combined sources10
Turni248 – 250Combined sources3
Beta strandi261 – 268Combined sources8
Beta strandi273 – 280Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AG5X-ray2.50A/B1-283[»]
3AG6X-ray1.85A/B1-283[»]
ProteinModelPortaliQ2FV22.
SMRiQ2FV22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IAA. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175517.
KOiK01918.
OMAiNIEMQIE.

Family and domain databases

CDDicd00560. PanC. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC. 1 hit.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2FV22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKLITTVKE MQHIVKAAKR SGTTIGFIPT MGALHDGHLT MVRESVSTND
60 70 80 90 100
ITIVSVFVNP LQFGPNEDFD AYPRQIDKDL ELVSEVGADI VFHPAVEDMY
110 120 130 140 150
PGELGIDVKV GPLADVLEGA KRPGHFDGVV TVVNKLFNIV MPDYAYFGKK
160 170 180 190 200
DAQQLAIVEQ MVKDFNHAVE IIGIDIVREA DGLAKSSRNV YLTEQERQEA
210 220 230 240 250
VHLSKSLLLA QALYQDGERQ SKVIIDRVTE YLESHISERI EEVAVYSYPQ
260 270 280
LVEQHEITGR IFISLAVKFS KARLIDNIII GAE
Length:283
Mass (Da):31,534
Last modified:March 21, 2006 - v1
Checksum:i553C07138066CC97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA. Translation: ABD31913.1.
RefSeqiWP_000163734.1. NC_007795.1.
YP_501370.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD31913; ABD31913; SAOUHSC_02918.
GeneIDi28379768.
3921369.
KEGGisao:SAOUHSC_02918.
PATRICi19583063. VBIStaAur99865_2637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA. Translation: ABD31913.1.
RefSeqiWP_000163734.1. NC_007795.1.
YP_501370.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AG5X-ray2.50A/B1-283[»]
3AG6X-ray1.85A/B1-283[»]
ProteinModelPortaliQ2FV22.
SMRiQ2FV22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93061.SAOUHSC_02918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD31913; ABD31913; SAOUHSC_02918.
GeneIDi28379768.
3921369.
KEGGisao:SAOUHSC_02918.
PATRICi19583063. VBIStaAur99865_2637.

Phylogenomic databases

eggNOGiENOG4108IAA. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175517.
KOiK01918.
OMAiNIEMQIE.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.
BRENDAi6.3.2.1. 3352.

Family and domain databases

CDDicd00560. PanC. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC. 1 hit.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPANC_STAA8
AccessioniPrimary (citable) accession number: Q2FV22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 21, 2006
Last modified: November 30, 2016
This is version 70 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

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.