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B8IHY4 (B8IHY4_METNO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pantothenate synthetase HAMAP MF_00158

Short name=PS HAMAP MF_00158
EC=6.3.2.1 HAMAP MF_00158
Alternative name(s):
Pantoate--beta-alanine ligase HAMAP MF_00158
Pantoate-activating enzyme HAMAP MF_00158
Gene names
Name:panC HAMAP MF_00158
Ordered Locus Names:Mnod_1014
OrganismMethylobacterium nodulans (strain ORS2060 / LMG 21967) [Complete proteome] [HAMAP]
Taxonomic identifier460265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length290 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 By similarity 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. HAMAP MF_00158

Ontologies

Keywords
   Biological processPantothenate biosynthesis HAMAP MF_00158
   Cellular componentCytoplasm HAMAP MF_00158
   LigandATP-binding HAMAP MF_00158
Nucleotide-binding
   Molecular functionLigase HAMAP MF_00158 EMBL ACL56022.1
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding42 – 498ATP By similarity HAMAP MF_00158
Nucleotide binding159 – 1624ATP By similarity HAMAP MF_00158
Nucleotide binding196 – 1994ATP By similarity HAMAP MF_00158

Sites

Active site491Proton donor By similarity HAMAP MF_00158
Binding site731Beta-alanine By similarity HAMAP MF_00158
Binding site731Pantoate By similarity HAMAP MF_00158
Binding site1651Pantoate By similarity HAMAP MF_00158
Binding site1881ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00158

Sequences

Sequence LengthMass (Da)Tools
B8IHY4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 597B99F86CCAB535

FASTA29030,725
        10         20         30         40         50         60 
MTALSPSPAA ETVARLGDVP ALRAQVRAWR AAGESVALVP TMGALHQGHL TLVRRARETC 

        70         80         90        100        110        120 
RRVVVSIFVN PTQFGPNEDF ARYPRDPERD IALLGEAGAD AAYLPDVGTM YPPGFATTVS 

       130        140        150        160        170        180 
VGGLTEVLCG PLRPGHFAGV ATVVTKLLLQ ALPDRALFGE KDYQQLQLIR RFVHDLDIPV 

       190        200        210        220        230        240 
AIEGVPTVRE ADGLALSSRN QYLSAAERAV APRLNAVLRR VAEAVRGGAE TAPALAEGRA 

       250        260        270        280        290 
TLEAAGFGPV QYLSVNDAES LAPLDRVAGP ARVLAAAYLG RTRLIDNVAV 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium nodulans ORS 2060."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ORS2060 / LMG 21967.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001349 Genomic DNA. Translation: ACL56022.1.
RefSeqYP_002496325.1. NC_011894.1.

3D structure databases

ProteinModelPortalB8IHY4.
SMRB8IHY4. Positions 24-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8IHY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7302558.
GenomeReviewsGene locus Mnod_1014 in contig CP001349_GR.
KEGGmno:Mnod_1014.
PATRIC22544232. VBIMetNod76414_1855.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMAEMDGLAM.
ProtClustDBPRK00380.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR004821. Cyt_trans-rel.
IPR003721. 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]
TIGRFAMsTIGR00125. Cyt_tran_rel. 1 hit.
TIGR00018. PanC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB8IHY4_METNO
AccessionPrimary (citable) accession number: B8IHY4
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: December 14, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)