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Q5X1M7

- PANC_LEGPA

UniProt

Q5X1M7 - PANC_LEGPA

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Protein

Pantothenate synthetase

Gene

panC

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed - 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 sitei152 – 1521PantoateUniRule annotation
Binding sitei175 – 1751ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368ATPUniRule annotation
Nucleotide bindingi146 – 1494ATPUniRule annotation
Nucleotide bindingi183 – 1864ATPUniRule 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

BioCyciLPNE297246:GCO9-3455-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:lpp2716
OrganismiLegionella pneumophila (strain Paris)
Taxonomic identifieri297246 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000000610: Chromosome

Organism-specific databases

LegioListilpp2716.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Pantothenate synthetasePRO_0000305469Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi297246.lpp2716.

Structurei

3D structure databases

ProteinModelPortaliQ5X1M7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
KOiK01918.
OMAiASSKENH.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

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

Q5X1M7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIFHNLNEW IRFRNSLSPD LSLGFAPTMG NLHAGHASLF LASSKENHYT
60 70 80 90 100
VSSLFVNPTQ FNNPDDYKHY PRTVDADLEL MTQNGVDFCI LPNENEIYTD
110 120 130 140 150
GYAYQVQENR LGQLMEGKHR PGHFNGVLTI VMKLFNLVKP TCAYFGEKDY
160 170 180 190 200
QQLLLIQGMV KALFMDIEIK SCPTVREKSG LACSSRNNRL TPSQREIADE
210 220 230 240 250
FAKIFHQNKS SAMISKELEA LGITVEYIEE FQGRRFAAVK IGDIRLIDNY

LL
Length:252
Mass (Da):28,765
Last modified:November 23, 2004 - v1
Checksum:iC8F6D7F9305C791F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628336 Genomic DNA. Translation: CAH13869.1.
RefSeqiYP_125021.1. NC_006368.1.

Genome annotation databases

EnsemblBacteriaiCAH13869; CAH13869; lpp2716.
GeneIDi3119604.
KEGGilpp:lpp2716.
PATRICi22326091. VBILegPne27771_3082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628336 Genomic DNA. Translation: CAH13869.1 .
RefSeqi YP_125021.1. NC_006368.1.

3D structure databases

ProteinModelPortali Q5X1M7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297246.lpp2716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH13869 ; CAH13869 ; lpp2716 .
GeneIDi 3119604.
KEGGi lpp:lpp2716.
PATRICi 22326091. VBILegPne27771_3082.

Organism-specific databases

LegioListi lpp2716.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175517.
KOi K01918.
OMAi ASSKENH.
OrthoDBi EOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci LPNE297246:GCO9-3455-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Paris.

Entry informationi

Entry nameiPANC_LEGPA
AccessioniPrimary (citable) accession number: Q5X1M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 23, 2004
Last modified: October 29, 2014
This is version 62 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