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Q1IHA8 (PANC_KORVE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:Acid345_4743
OrganismKoribacter versatilis (strain Ellin345) [Reference proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305381

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IHA8 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 5250848795BD6034

FASTA29131,878
        10         20         30         40         50         60 
MRVVRTIAEM QAICRTLHRE GKSIGLVPTM GALHAGHISL VRTARTQNDS VVVSIFVNPI 

        70         80         90        100        110        120 
QFGPNEDLAK YPRTFEQDCA QLDHEGVDFV FSPGVEEMYP EGTATFVHVD GLSEKLDGRS 

       130        140        150        160        170        180 
RPGHFKGVTT VVSKLFHIIP ADHAYFGQKD AAQVAVIRKM VRDQNFDIDL MICPIVREKD 

       190        200        210        220        230        240 
GLALSSRNAY LDPTQRQQAL VLHRALMRVQ MLADTGHTDA YYLAEAGRAV IAEEPGAKLD 

       250        260        270        280        290 
YLEIVDPNTL EPITEIGKGA LVAVAAQIGN TRLIDNLVLQ AAGNARGPRT S 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF43742.1.
RefSeqYP_593816.1. NC_008009.1.

3D structure databases

ProteinModelPortalQ1IHA8.
SMRQ1IHA8. Positions 1-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204669.Acid345_4743.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF43742; ABF43742; Acid345_4743.
GeneID4070681.
KEGGaba:Acid345_4743.
PATRIC31986925. VBICanKor57425_5069.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAECPIVRE.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycKVER204669:GHL8-4794-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_KORVE
AccessionPrimary (citable) accession number: Q1IHA8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways