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Protein

Pantothenate synthetase

Gene

panC

Organism
Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
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: (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 sitei34Proton donorUniRule annotation1
Binding sitei58Beta-alanineUniRule annotation1
Binding sitei58PantoateUniRule annotation1
Binding sitei150PantoateUniRule annotation1
Binding sitei173ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi27 – 34ATPUniRule annotation8
Nucleotide bindingi144 – 147ATPUniRule annotation4
Nucleotide bindingi181 – 184ATPUniRule 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:DehaBAV1_0728
OrganismiDehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
Taxonomic identifieri216389 [NCBI]
Taxonomic lineageiBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

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_10000768531 – 277Pantothenate synthetaseAdd BLAST277

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA5FR69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000175516.
KOiK01918.
OMAiDMAMLEN.

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.

A5FR69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIIRTVDEM KKLHREICGP VGLVPTMGYL HEGHLSLVRA SKKQDINTVA
60 70 80 90 100
SIFVNPTQFG PHEDFKKYPR DEKRDMAMLE NAGVDYVFAP SVEDMYPAGF
110 120 130 140 150
DSWVEPGILQ QCLEGAIRPG HFRGVCTVVA KLFTIIRPDR AYFGQKDYQQ
160 170 180 190 200
YLIIKRMASD LNLDVSVEML PIIRENDGLA LSSRNTYLSP AERQAALVLY
210 220 230 240 250
RSLLTARSLF DEKEHRAEVI RKKMTDVIQH ESMAEIDYVS LSHQDTLCES
260 270
DEVSAKTIAL VAARFGKTRL IDNMFLA
Length:277
Mass (Da):31,456
Last modified:June 12, 2007 - v1
Checksum:i25D411BF57C6880F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000688 Genomic DNA. Translation: ABQ17312.1.
RefSeqiWP_011929054.1. NC_009455.1.

Genome annotation databases

EnsemblBacteriaiABQ17312; ABQ17312; DehaBAV1_0728.
KEGGideb:DehaBAV1_0728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000688 Genomic DNA. Translation: ABQ17312.1.
RefSeqiWP_011929054.1. NC_009455.1.

3D structure databases

ProteinModelPortaliA5FR69.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ17312; ABQ17312; DehaBAV1_0728.
KEGGideb:DehaBAV1_0728.

Phylogenomic databases

HOGENOMiHOG000175516.
KOiK01918.
OMAiDMAMLEN.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.

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_DEHMB
AccessioniPrimary (citable) accession number: A5FR69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 66 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.