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A1UMI0 (PANC_MYCSK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:Mkms_4848
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length313 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 – 313313Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305489

Regions

Nucleotide binding43 – 508ATP By similarity
Nucleotide binding161 – 1644ATP By similarity
Nucleotide binding198 – 2014ATP By similarity

Sites

Active site501Proton donor By similarity
Binding site751Beta-alanine By similarity
Binding site751Pantoate By similarity
Binding site1671Pantoate By similarity
Binding site1901ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1UMI0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F712971E5184A02D

FASTA31333,668
        10         20         30         40         50         60 
MTARRPTRFA KGELNVYRAP RDVTDVTRAL RSTGRRVVLV PTMGALHEGH LTLIRAAKRV 

        70         80         90        100        110        120 
QGAVVVVSIF VNPLQFGAGE DLDAYPRTLD DDLAALRAEG VEIAFTPTVG DMYPDGTRTS 

       130        140        150        160        170        180 
VHPGPLGDDL EGASRPGHFA GVLTVVCKLL HIVRPDRAFF GEKDYQQLVL IRQMVTDLNI 

       190        200        210        220        230        240 
DTKIVGVPTV READGLALSS RNRYLDEVER EQAGALSAAL LAGMYAASNG AAATLDAARA 

       250        260        270        280        290        300 
VLDEVPAIEV DYLQVRDPML GPVPHEGAAR LLVAARLGQT RLLDNIAVDI GASDGIDGHP 

       310 
RVGSPDHQLP WRN 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
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., Kiss H., 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., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL94038.1.
RefSeqYP_940828.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UMI0.
SMRA1UMI0. Positions 9-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189918.Mkms_4848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL94038; ABL94038; Mkms_4848.
GeneID4616263.
KEGGmkm:Mkms_4848.
PATRIC18108752. VBIMycSp70743_5384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycMSP189918:GH4X-4896-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_MYCSK
AccessionPrimary (citable) accession number: A1UMI0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: June 11, 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