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A9B3W0 (PANC_HERA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Haur_3460
OrganismHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785) [Complete proteome] [HAMAP]
Taxonomic identifier316274 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length276 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 MF_00158

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP MF_00158

Subcellular location

Cytoplasm Potential HAMAP MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158

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-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Pantothenate synthetase HAMAP MF_00158
PRO_1000097075

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding143 – 1464ATP By similarity
Nucleotide binding180 – 1834ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1491Pantoate By similarity
Binding site1721ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9B3W0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 799FF0D743F2832D

FASTA27630,089
        10         20         30         40         50         60 
MQVVTTIEEV RAARRQWAEV GFVPTMGFLH AGHLSLVQQS KAENGVAIAS IFVNPTQFGP 

        70         80         90        100        110        120 
NEDFASYPRD TPRDLALLEA AGCDLVWMPS VEEIYPAGFS SYVEVEGVTA PLEGARRPGH 

       130        140        150        160        170        180 
FRGVATVVTK LFNVVQPTKA YFGQKDAQQT VVIRQFVRDL AMPVEVVIAP TIREADGLAM 

       190        200        210        220        230        240 
SSRNSYLNAE QRAAAPVLYR ALTAAQTAYA AGQTDAEAIR QLMLETLAQE PLAQVDYVSI 

       250        260        270 
ADPRSLQELT TIDQQGVLVS LAVRIGKTRL IDNLVM 

« Hide

References

[1]"Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Bryant D.A., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23779 / DSM 785.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000875 Genomic DNA. Translation: ABX06096.1.
RefSeqYP_001546224.1. NC_009972.1.

3D structure databases

ProteinModelPortalA9B3W0.
SMRA9B3W0. Positions 1-275.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9B3W0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5735321.
GenomeReviewsGene locus Haur_3460 in contig CP000875_GR.
KEGGhau:Haur_3460.
PATRIC22124079. VBIHerAur93466_3559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMALNMPIQI.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycHAUR316274:HAUR_3460-MONOMER.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01918.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. PanC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_HERA2
AccessionPrimary (citable) accession number: A9B3W0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families