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A7ZW82

- PANC_ECOHS

UniProt

A7ZW82 - PANC_ECOHS

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Protein

Pantothenate synthetase

Gene

panC

Organism
Escherichia coli O9:H4 (strain HS)
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 sitei37 – 371Proton donorUniRule annotation
Binding sitei61 – 611Beta-alanineUniRule annotation
Binding sitei61 – 611PantoateUniRule annotation
Binding sitei155 – 1551PantoateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATPUniRule annotation
Nucleotide bindingi149 – 1524ATPUniRule annotation
Nucleotide bindingi186 – 1894ATPUniRule 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

BioCyciECOL331112:GHHI-136-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:EcHS_A0137
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: Chromosome

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 – 283283Pantothenate synthetasePRO_1000097062Add
BLAST

Proteomic databases

PRIDEiA7ZW82.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A0137.

Structurei

3D structure databases

ProteinModelPortaliA7ZW82.
SMRiA7ZW82. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
KOiK01918.
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.

A7ZW82-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV
60 70 80 90 100
VVVSIFVNPM QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP
110 120 130 140 150
NGTETHTYVD VPGLSTMLEG ASRPGHFRGV STIVSKLFNL VQPDIACFGE
160 170 180 190 200
KDFQQLALIR KMVADMGFDI EIVGVPIMRA KDGLALSSRN GYLTAEQRKI
210 220 230 240 250
APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA DDIQIRDADT
260 270 280
LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA
Length:283
Mass (Da):31,598
Last modified:October 23, 2007 - v1
Checksum:i4246647C6FDAFB20
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV04536.1.
RefSeqiYP_001456919.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV04536; ABV04536; EcHS_A0137.
GeneIDi5593359.
KEGGiecx:EcHS_A0137.
PATRICi18310269. VBIEscCol77814_0138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV04536.1 .
RefSeqi YP_001456919.1. NC_009800.1.

3D structure databases

ProteinModelPortali A7ZW82.
SMRi A7ZW82. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A0137.

Proteomic databases

PRIDEi A7ZW82.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV04536 ; ABV04536 ; EcHS_A0137 .
GeneIDi 5593359.
KEGGi ecx:EcHS_A0137.
PATRICi 18310269. VBIEscCol77814_0138.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci ECOL331112:GHHI-136-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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiPANC_ECOHS
AccessioniPrimary (citable) accession number: A7ZW82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 53 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