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Protein

Pantothenate synthetase

Gene

panC

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
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), 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 sitei36Proton donorUniRule annotation1
Binding sitei60Beta-alanineUniRule annotation1
Binding sitei60PantoateUniRule annotation1
Binding sitei153PantoateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 36ATPUniRule annotation8
Nucleotide bindingi147 – 150ATPUniRule annotation4
Nucleotide bindingi184 – 187ATPUniRule 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:FTT_1390
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 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_00003054501 – 261Pantothenate synthetaseAdd BLAST261

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi177416.FTT_1390.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi7 – 15Combined sources9
Beta strandi23 – 28Combined sources6
Helixi34 – 46Combined sources13
Beta strandi48 – 54Combined sources7
Helixi58 – 60Combined sources3
Helixi64 – 69Combined sources6
Helixi74 – 83Combined sources10
Beta strandi87 – 90Combined sources4
Helixi94 – 97Combined sources4
Beta strandi104 – 108Combined sources5
Helixi111 – 114Combined sources4
Helixi117 – 120Combined sources4
Helixi124 – 139Combined sources16
Beta strandi142 – 147Combined sources6
Helixi151 – 163Combined sources13
Beta strandi169 – 173Combined sources5
Helixi186 – 190Combined sources5
Helixi193 – 207Combined sources15
Helixi214 – 222Combined sources9
Turni223 – 225Combined sources3
Beta strandi227 – 234Combined sources8
Beta strandi237 – 244Combined sources8
Beta strandi247 – 254Combined sources8
Turni255 – 257Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N8HX-ray2.00A/B1-261[»]
3QTTX-ray2.60A/B1-258[»]
5HG0X-ray2.40A/B1-261[»]
ProteinModelPortaliQ5NF57.
SMRiQ5NF57.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5NF57.

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107R03. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175517.
KOiK01918.
OMAiLIDHIKY.

Family and domain databases

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.

Q5NF57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIADNIKQF HSIRNSLIKQ QKIGFVPTMG ALHNGHISLI KKAKSENDVV
60 70 80 90 100
IVSIFVNPTQ FNNPNDYQTY PNQLQQDIQI LASLDVDVLF NPSEKDIYPD
110 120 130 140 150
GNLLRIEPKL EIANILEGKS RPGHFSGMLT VVLKLLQITK PNNLYLGEKD
160 170 180 190 200
YQQVMLIKQL VKDFFINTKI IVCPTQRQPS GLPLSSRNKN LTSTDIEIAN
210 220 230 240 250
KIYEILRQDD FSNLEELTNK INSTGAKLQY IQKLNNRIFL AFYIGKVRLI
260
DNFLKETGPS C
Length:261
Mass (Da):29,715
Last modified:February 1, 2005 - v1
Checksum:i9EF115B43EDC2FDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG46023.1.
RefSeqiWP_003022190.1. NZ_CP010290.1.
YP_170335.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG46023; CAG46023; FTT_1390.
GeneIDi3191378.
KEGGiftu:FTT_1390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG46023.1.
RefSeqiWP_003022190.1. NZ_CP010290.1.
YP_170335.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N8HX-ray2.00A/B1-261[»]
3QTTX-ray2.60A/B1-258[»]
5HG0X-ray2.40A/B1-261[»]
ProteinModelPortaliQ5NF57.
SMRiQ5NF57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177416.FTT_1390.

Protocols and materials databases

DNASUi3191378.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG46023; CAG46023; FTT_1390.
GeneIDi3191378.
KEGGiftu:FTT_1390.

Phylogenomic databases

eggNOGiENOG4107R03. Bacteria.
COG0414. LUCA.
HOGENOMiHOG000175517.
KOiK01918.
OMAiLIDHIKY.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.

Miscellaneous databases

EvolutionaryTraceiQ5NF57.

Family and domain databases

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_FRATT
AccessioniPrimary (citable) accession number: Q5NF57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 1, 2005
Last modified: November 2, 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.