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P57035 (PANC_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:NMA1089
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length278 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 – 278278Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128247

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding144 – 1474ATP By similarity
Nucleotide binding181 – 1844ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1501Pantoate By similarity
Binding site1731ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P57035 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 4D19DC9D5501FBF8

FASTA27831,021
        10         20         30         40         50         60 
MQIIHTIQEL RAWRKNAGTV AFVPTMGNLH EGHLALVREA KKRADNVVVS IFVNRLQFGQ 

        70         80         90        100        110        120 
GEDFDKYPRT LQQDADKLEA EGVAVVFAPD EKELYPNVEQ RYNVEPPNLQ NELCGKFRPG 

       130        140        150        160        170        180 
HFLGVATVVS KLFNIVAPDV ACFGKKDYQQ LAVIKGLTED LNFDVEIVPV DTGRAEDGLA 

       190        200        210        220        230        240 
LSSRNQYLSA AERDEAPRLY RELKAVAESL AQGSLDYAGL EKRAVQSLTE YGWVVDYVEI 

       250        260        270 
RRVDTLEVAR AGDKKLVVLA AARLGTTRLI DNLEIKLP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM08300.1.
PIRF81874.
RefSeqYP_002342495.1. NC_003116.1.

3D structure databases

ProteinModelPortalP57035.
SMRP57035. Positions 1-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA1089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM08300; CAM08300; NMA1089.
GeneID907059.
KEGGnma:NMA1089.
PATRIC20363102. VBINeiMen132687_1259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAEIDYVEV.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1004-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_NEIMA
AccessionPrimary (citable) accession number: P57035
Secondary accession number(s): A1IRB4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: May 14, 2014
This is version 82 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