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Protein

Pantothenate synthetase

Gene

panC

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
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

Pathway: (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341Proton donorUniRule annotation
Binding sitei61 – 611Beta-alanineUniRule annotation
Binding sitei61 – 611PantoateUniRule annotation
Binding sitei154 – 1541PantoateUniRule annotation
Binding sitei177 – 1771ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 348ATPUniRule annotation
Nucleotide bindingi148 – 1514ATPUniRule annotation
Nucleotide bindingi185 – 1884ATPUniRule annotation

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

BioCyciSAVE227882:GJU1-4741-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:SAV_4687
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
ProteomesiUP000000428 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Pantothenate synthetasePRO_0000305563Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi227882.SAV_4687.

Structurei

3D structure databases

ProteinModelPortaliQ82EC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiGGEPQVR.
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]
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q82EC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTLLRTAD ELHARVRHGR RAVVMTMGAL HEGHATLIRT AREIAGAEGE
60 70 80 90 100
VVVTVFVNPL QFGRGEDLDR YPRTLDADLK IAEAAGADVV FAPSADEVYP
110 120 130 140 150
GGEPQVRISA GPMGERLEGA FRPGHFDGML TVVGKLLHLT RPDVALYGQK
160 170 180 190 200
DAQQLALIRR MARDLNFGVE IVGVPTVRED DGLALSSRNR YLAADERRTA
210 220 230 240 250
LALSQALFAG RDRHAAQEAL RARAREVPAT RARAEALSAI GESRAAADAH
260 270 280 290 300
AVAKATPAGT SGPAAVRCAA RLVLEEAARL QPPLVLDYLG LVDPSDFTEI
310 320 330
PDDFTGEAVL AVAARVGTTR LIDNIPLTFG AAS
Length:333
Mass (Da):35,472
Last modified:June 1, 2003 - v1
Checksum:i6CC22E59257E85D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC72399.1.
RefSeqiNP_825864.1. NC_003155.4.
WP_010986111.1. NZ_BAVY01000024.1.

Genome annotation databases

EnsemblBacteriaiBAC72399; BAC72399; SAV_4687.
KEGGisma:SAV_4687.
PATRICi23723249. VBIStrAve112782_5003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC72399.1.
RefSeqiNP_825864.1. NC_003155.4.
WP_010986111.1. NZ_BAVY01000024.1.

3D structure databases

ProteinModelPortaliQ82EC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_4687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC72399; BAC72399; SAV_4687.
KEGGisma:SAV_4687.
PATRICi23723249. VBIStrAve112782_5003.

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiGGEPQVR.
OrthoDBiEOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.
BioCyciSAVE227882:GJU1-4741-MONOMER.

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]
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
    Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
    Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
  2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
    Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
    Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Entry informationi

Entry nameiPANC_STRAW
AccessioniPrimary (citable) accession number: Q82EC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 75 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, Reference 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.