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B2UND0 (PANC_AKKM8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:Amuc_0404
OrganismAkkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]
Taxonomic identifier349741 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia

Protein attributes

Sequence length281 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 – 281281Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097026

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding150 – 1534ATP By similarity
Nucleotide binding187 – 1904ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site641Beta-alanine By similarity
Binding site641Pantoate By similarity
Binding site1561Pantoate By similarity
Binding site1791ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UND0 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: CC39BF5AD725D307

FASTA28130,917
        10         20         30         40         50         60 
MQTFSTKAQL RAALLKHHRK HDHVVLVPTM GALHAGHRAL LEQARKLAGE DGVVVASIFV 

        70         80         90        100        110        120 
NPIQFNNSSD LQTYPRTPEK DLEVCEGAGV DYVFSPAPEE MYSGERSIAV EESFLSATLC 

       130        140        150        160        170        180 
GASRPGHFSG VCTVLAKLFN LVQPTDAIFG KKDYQQLAII RRMVRDLDFP VRIHGAEIVR 

       190        200        210        220        230        240 
HGNGLAYSSR NARLTPEQKE QAVVIRQAML QARDEFQAGA DASKVKEHAA AMIEGVPGTR 

       250        260        270        280 
IDYLEIVDAE TMQPVAENRK PALMAAAVYF GDVRLIDNIE L 

« Hide

References

[1]"Complete sequence of Akkermansia muciniphila ATCC BAA-835."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-835.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001071 Genomic DNA. Translation: ACD04242.1.
RefSeqYP_001877023.1. NC_010655.1.

3D structure databases

ProteinModelPortalB2UND0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349741.Amuc_0404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD04242; ACD04242; Amuc_0404.
GeneID6274820.
KEGGamu:Amuc_0404.
PATRIC20833404. VBIAkkMuc16855_0458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAQKDAQQF.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycAMUC349741:GHZ7-424-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_AKKM8
AccessionPrimary (citable) accession number: B2UND0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 39 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