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Protein

Pantothenate synthetase

Gene

panC

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei36 – 361Proton donorUniRule annotation
Binding sitei60 – 601Beta-alanineUniRule annotation
Binding sitei60 – 601PantoateUniRule annotation
Binding sitei153 – 1531PantoateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368ATPUniRule annotation
Nucleotide bindingi147 – 1504ATPUniRule annotation
Nucleotide bindingi184 – 1874ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. pantoate-beta-alanine ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciFTUL393115:GJUT-1421-MONOMER.
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:FTF1390
OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
Taxonomic identifieri393115 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001821 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Pantothenate synthetasePRO_0000305451Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi393115.FTF1390.

Structurei

3D structure databases

ProteinModelPortaliQ14GL0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
KOiK01918.
OMAiKNIEQFN.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
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.

Q14GL0-1 [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:August 21, 2006 - v1
Checksum:i9EF115B43EDC2FDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL09406.1.
RefSeqiYP_667467.1. NC_008245.1.

Genome annotation databases

EnsemblBacteriaiCAL09406; CAL09406; FTF1390.
GeneIDi4200091.
KEGGiftf:FTF1390.
PATRICi17961902. VBIFraTul133500_1599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL09406.1.
RefSeqiYP_667467.1. NC_008245.1.

3D structure databases

ProteinModelPortaliQ14GL0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi393115.FTF1390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL09406; CAL09406; FTF1390.
GeneIDi4200091.
KEGGiftf:FTF1390.
PATRICi17961902. VBIFraTul133500_1599.

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
KOiK01918.
OMAiKNIEQFN.
OrthoDBiEOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.
BioCyciFTUL393115:GJUT-1421-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
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...

Publicationsi

  1. "Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
    Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
    PLoS ONE 2:E352-E352(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FSC 198.

Entry informationi

Entry nameiPANC_FRAT1
AccessioniPrimary (citable) accession number: Q14GL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 2007
Last sequence update: August 21, 2006
Last modified: January 6, 2015
This is version 58 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.