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B5F832

- PANC_SALA4

UniProt

B5F832 - PANC_SALA4

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Protein
Pantothenate synthetase
Gene
panC, SeAg_B0215
Organism
Salmonella agona (strain SL483)
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 By similarity.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Proton donor By similarity
Binding sitei61 – 611Beta-alanine By similarity
Binding sitei61 – 611Pantoate By similarity
Binding sitei155 – 1551Pantoate By similarity
Binding sitei178 – 1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATP By similarity
Nucleotide bindingi149 – 1524ATP By similarity
Nucleotide bindingi186 – 1894ATP By similarity

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

BioCyciSENT454166:GHBA-210-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetase (EC:6.3.2.1)
Short name:
PS
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene namesi
Name:panC
Ordered Locus Names:SeAg_B0215
OrganismiSalmonella agona (strain SL483)
Taxonomic identifieri454166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008819: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 284284Pantothenate synthetaseUniRule annotation
PRO_1000097097Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi454166.SeAg_B0215.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
OMAiECPIVRE.
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.

B5F832-1 [UniParc]FASTAAdd to Basket

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MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV    50
VIVSIFVNPM QFDRPDDLVR YPRTLQEDCE KLNKRKVDYV FAPAVEEIYP 100
QGLEGQTYVD VPGLSTMLEG ASRPGHFRGV STIVSKLFNL IQPDIACFGE 150
KDFQQLALIR KMVADMSYDI EIVGVPIIRA KDGLALSSRN GYLTAEQRKI 200
APGLHNVMNS IAEKLIAGNR ELQEIIAIAE QELNEKGFRA DDIQIRDADT 250
LQELTETSKR AVILAAAWLG QARLIDNQSV TLAQ 284
Length:284
Mass (Da):31,824
Last modified:October 14, 2008 - v1
Checksum:iA23EBB121E950104
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001138 Genomic DNA. Translation: ACH51091.1.
RefSeqiYP_002145182.1. NC_011149.1.

Genome annotation databases

EnsemblBacteriaiACH51091; ACH51091; SeAg_B0215.
PATRICi18478800. VBISalEnt65316_0243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001138 Genomic DNA. Translation: ACH51091.1 .
RefSeqi YP_002145182.1. NC_011149.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 454166.SeAg_B0215.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH51091 ; ACH51091 ; SeAg_B0215 .
PATRICi 18478800. VBISalEnt65316_0243.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175517.
OMAi ECPIVRE.
OrthoDBi EOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci SENT454166:GHBA-210-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR004821. Cyt_trans-like.
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 TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SL483.

Entry informationi

Entry nameiPANC_SALA4
AccessioniPrimary (citable) accession number: B5F832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 43 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 By similarity.

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

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