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Reviewed, UniProtKB/Swiss-Prot B6YS36 (PANB_AZOPC)

Last modified September 22, 2009. Version 10. 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:
    3-methyl-2-oxobutanoate hydroxymethyltransferase
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase
      Short name=KPHMT
Gene names
Name: panB
Ordered Locus Names: CFPG_745
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

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Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2722723-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096941

Regions

Region52 – 532Alpha-ketoisovalerate binding By similarity

Sites

Active site1901Proton acceptor By similarity
Metal binding521Magnesium By similarity
Metal binding911Magnesium By similarity
Metal binding1231Magnesium By similarity
Binding site911Alpha-ketoisovalerate By similarity
Binding site1211Alpha-ketoisovalerate By similarity

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Sequences

Sequence LengthMass (Da)Tools
B6YS36-1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: C7B061F274FCAC2C

FASTA27229,935
        10         20         30         40         50         60 
MPLHTGDIRK ITIQHLIEMK SYCEKISMIT AYDYSMASII DKTGMDIVLV GDSASNVMAG 

        70         80         90        100        110        120 
NTTTLPITLD QMIWYAQSVR KAVQRALLCV DMPFGSYQGN SKKAVHSAIR IIKETGADAI 

       130        140        150        160        170        180 
KIEGGKEICE SVKRILSAGI PTMGHLGLTP QSINKLGGYS IQAKKKDEAQ RLMEDACLLE 

       190        200        210        220        230        240 
ELGCFSIVLE KIPAKLGKQV SEKLSIPLIG IGAGPYVDGQ VLVLQDMLGI NKSFAPRFLR 

       250        260        270 
CYADLYNVIK KSVEHYVQDV KNANFPNEQE SY

« Hide

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References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AP010656 Genomic DNA. Translation: BAG84008.1.
RefSeqYP_002309419.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7039329.
GenomeReviewsGene locus CFPG_745 in contig AP010656_GR.
KEGGaps:CFPG_745.

Organism-specific databases

CMRSearch...

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...

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Entry information

Entry namePANB_AZOPC
AccessionPrimary (citable) accession number: B6YS36
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: September 22, 2009
This is version 10 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