Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0ANX4 (PANC_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Mmar10_1721
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length288 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
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 – 288288Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305479

Regions

Nucleotide binding35 – 428ATP By similarity
Nucleotide binding152 – 1554ATP By similarity
Nucleotide binding189 – 1924ATP By similarity

Sites

Active site421Proton donor By similarity
Binding site661Beta-alanine By similarity
Binding site661Pantoate By similarity
Binding site1581Pantoate By similarity
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ANX4 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 7A8E2AFCDAE9CF11

FASTA28830,943
        10         20         30         40         50         60 
MITQQIPHAT TISALRTRVR SWREDRLSVG FVPTMGALHD GHVSLVRLAK AQCDRVVASV 

        70         80         90        100        110        120 
FVNPKQFAPG EDLDAYPRTL IDDAEKLTDA KCDLIYLPTP EAMYPDGYSA GVTLKGPALG 

       130        140        150        160        170        180 
LESAIRPHFF DGVATVVTKL FNQVRPDMAF FGEKDYQQLL VIRQLVKDLD FPINVLAGET 

       190        200        210        220        230        240 
GRDRDGLALS SRNAYLDSDQ RTRAGQLNLI LKAFAAALSG GASTSDATAT ALAAASDAFD 

       250        260        270        280 
AVDYVEARCA ATLAELGDGP IDRPVRVLAA VRLGSTRLID NMAANPPA 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000449 Genomic DNA. Translation: ABI66013.1.
RefSeqYP_756951.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0ANX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394221.Mmar10_1721.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI66013; ABI66013; Mmar10_1721.
GeneID4286177.
KEGGmmr:Mmar10_1721.
PATRIC22451562. VBIMarMar77530_1765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMADYFEARH.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-1754-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_MARMM
AccessionPrimary (citable) accession number: Q0ANX4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 50 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