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Reviewed, UniProtKB/Swiss-Prot Q5NL16 (PANB2_ZYMMO)

Last modified November 3, 2009. Version 31. 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 2
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 2
      Short name=KPHMT 2
Gene names
Name: panB2
Ordered Locus Names: ZMO1970
OrganismZymomonas mobilis [Complete proteome] [HAMAP]
Taxonomic identifier542 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length273 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 – 2732733-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156
PRO_0000297419

Regions

Region50 – 512Alpha-ketoisovalerate binding By similarity

Sites

Active site1881Proton acceptor By similarity
Metal binding501Magnesium By similarity
Metal binding891Magnesium By similarity
Metal binding1211Magnesium By similarity
Binding site891Alpha-ketoisovalerate By similarity
Binding site1191Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NL16-1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 4F88F3A83CFD0AA9

FASTA27329,231
        10         20         30         40         50         60 
MSAIPSSNKR RTIPELRARK GKSPIVALTA YSALTARFVD PYADFILVGD SLAMVEHGMA 

        70         80         90        100        110        120 
TTIGASLDMM ILHGQSVMRG SEKAAVVIDM PFGSYEASPQ EAYHNAVRIL SETGCSAVKL 

       130        140        150        160        170        180 
EGGSHLAPVI AFLTARGVPV MGHIGLTPQY VQTLGGFKIQ GHSSEQQDKI KQDALDFEAA 

       190        200        210        220        230        240 
GAFSVVLEGV TEPLAREITD NIAIPTIGIG ASSYCDGQVL VLEDMLGFND KVPRFVKKFA 

       250        260        270 
HLGDDIKKAV SDYATAVSNR SFPAEDNIYR PKS 

« Hide

References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

AE008692 Genomic DNA. Translation: AAV90594.1.
RefSeqYP_163705.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3188177.
GenomeReviewsGene locus ZMO1970 in contig AE008692_GR.
KEGGzmo:ZMO1970.
NMPDRfig|264203.3.peg.1382.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5NL16.
OMALVVVDMP.

Enzyme and pathway databases

BioCycZMOB264203:ZMO1970-MON.
BRENDA2.1.2.11. 1658.

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 namePANB2_ZYMMO
AccessionPrimary (citable) accession number: Q5NL16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 1, 2005
Last modified: November 3, 2009
This is version 31 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