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Reviewed, UniProtKB/Swiss-Prot Q391N3 (PANB1_BURS3)

Last modified November 3, 2009. Version 29. 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

Names and origin

Protein namesRecommended name:
    3-methyl-2-oxobutanoate hydroxymethyltransferase 1
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 1
      Short name=KPHMT 1
Gene names
Name: panB1
Ordered Locus Names: Bcep18194_B2722
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate By similarity.

Catalytic activity

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP MF_00156

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP MF_00156

Subunit structure

Homodecamer; pentamer of dimers By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the panB family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionMethyltransferase
Transferase
   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 function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2852853-methyl-2-oxobutanoate hydroxymethyltransferase 1 HAMAP MF_00156
PRO_0000297235

Regions

Region49 – 502Alpha-ketoisovalerate binding By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding491Magnesium By similarity
Metal binding881Magnesium By similarity
Metal binding1201Magnesium By similarity
Binding site881Alpha-ketoisovalerate By similarity
Binding site1181Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q391N3-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 31DAF824721B4C5B

FASTA28529,835
        10         20         30         40         50         60 
MSAHTRTTRK TVTAIRSTKG IGSLVSLTAY SAPMAKLVDE VADVIIVGDS VGMVLYGMPD 

        70         80         90        100        110        120 
TLRVTLDMMI AHGAAVVRGA AQACVVVDLP FSTYQESPAQ AYRSAARLLA ETGAQGVKLE 

       130        140        150        160        170        180 
GGTEMADAIR FLTERGIPVM AHVGLMPQQA NATGGFRAQG MDPRSAAQVF DAACSAEQAG 

       190        200        210        220        230        240 
AFSVVIEGTA EALARHITET LTIPTIGIGA SPACDGQVLV TEDMIGAFDA YTPRFVKRYA 

       250        260        270        280 
DANAVMRDAI RQYAHDVRQG VFPEPAHCFG YGKPLQLVGA ADAAA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia sp. 383."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000152 Genomic DNA. Translation: ABB12833.1.
RefSeqYP_373477.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ391N3.

Genome annotation databases

GeneID3754489.
GenomeReviewsGene locus Bcep18194_B2722 in contig CP000152_GR.
KEGGbur:Bcep18194_B2722.
NMPDRfig|269483.3.peg.2485.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ391N3.
OMALVVVDMP.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_B2722-MON.

Family and domain databases

HAMAPMF_00156.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB1_BURS3
AccessionPrimary (citable) accession number: Q391N3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: November 22, 2005
Last modified: November 3, 2009
This is version 29 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)

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