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Reviewed, UniProtKB/Swiss-Prot Q5NXQ2 (PANC_AZOSE)

Last modified February 9, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: AZOSEA40370
ORF Names: ebA7120
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

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Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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: 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: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Pantothenate synthetase HAMAP MF_00158
PRO_0000305395

Regions

Nucleotide binding27 – 348ATP By similarity
Nucleotide binding145 – 1484ATP By similarity
Nucleotide binding182 – 1854ATP By similarity

Sites

Active site341Proton donor By similarity
Binding site581Beta-alanine By similarity
Binding site581Pantoate By similarity
Binding site1511Pantoate By similarity
Binding site1741ATP; via amide nitrogen and carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5NXQ2-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C522DD0EE70341F3

FASTA27630,487
        10         20         30         40         50         60 
MQIHTTIQSL RAARAAVSGK VALVPTMGNL HDGHIALMRQ ATGHADSIVA SIFVNRLQFG 

        70         80         90        100        110        120 
PRDDFDRYPR TFKADCERLE AAGVAHVFAP DEGEMYPQPQ QYHVDPAPAH VTILEGEFRP 

       130        140        150        160        170        180 
DHFRGVATVV LKLLNIVRPD VALFGKKDYQ QLMVLTNMVR ELAVAVEVVP GETIRATDGL 

       190        200        210        220        230        240 
ALSSRNGYLS AEERVEAPRL YRELARVRDA VRDGDRDFLK LETEAVAGLA AHGWHPDYIA 

       250        260        270 
VRRRADLQPP GDANDPLVVL AAAKLGHTRL IDNLEI

« Hide

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References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI10162.1.
RefSeqYP_161063.1.

3D structure databases

HSSPHSSP built from PDB template 1N2E based on UniProtKB P0A5R0.
SMRQ5NXQ2. Positions 1-276.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5NXQ2.

Genome annotation databases

GeneID3181680.
GenomeReviewsGene locus AZOSEA40370 in contig CR555306_GR.
KEGGeba:ebA7120.
NMPDRfig|76114.4.peg.4053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHBG428839.
OMAMPIQIIG.

Enzyme and pathway databases

BioCycASP76114:EBA7120-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.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePANC_AZOSE
AccessionPrimary (citable) accession number: Q5NXQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents