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

Q9AMR9 (PANC1_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. 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 1

Short name=PS 1
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase 1
Pantoate-activating enzyme 1
Gene names
Name:panC1
Ordered Locus Names:blr2102
ORF Names:id912
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length283 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 – 283283Pantothenate synthetase 1 HAMAP-Rule MF_00158
PRO_0000128208

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
Q9AMR9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A2CA526734D9A607

FASTA28331,322
        10         20         30         40         50         60 
MKVITKVAEL RRALADVRNA EKRIGFVPTM GYLHDGHLAL ISASREHCDV TVVSIFVNPT 

        70         80         90        100        110        120 
QFGPNEDLSR YPRDFARDEA LCGSAGVSII FAPSAEEIYP AQFESFVEPG ELAKPLCGAF 

       130        140        150        160        170        180 
RPGHFRGVAT VVCKLFNMVQ PDVAYFGQKD FQQCAVIRRM TVDLNLPIEI VTVPTVREPD 

       190        200        210        220        230        240 
GLAMSSRNRY LCPEERDRSL AISRGLFAAA HEFASGERDA ATLIALARRH LERVDRLQYL 

       250        260        270        280 
ELVDPGTLRI ADSPLRYPAV LCVAAYVGST RLIDNVVLSW SPS 

« Hide

References

« Hide 'large scale' references
[1]"Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA region of the Bradyrhizobium japonicum chromosome."
Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R., Hennecke H.
J. Bacteriol. 183:1405-1412(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110spc4.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF322013 Genomic DNA. Translation: AAG61078.1.
BA000040 Genomic DNA. Translation: BAC47367.1.
RefSeqNP_768742.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ9AMR9.
SMRQ9AMR9. Positions 1-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr2102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC47367; BAC47367; BAC47367.
GeneID1055455.
KEGGbja:blr2102.
PATRIC21187544. VBIBraJap65052_2034.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OrthoDBEOG6Z6FZ4.
PhylomeDBQ9AMR9.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-2122-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]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC1_BRADU
AccessionPrimary (citable) accession number: Q9AMR9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 72 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