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Q8YWS8 (PANB_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:all1522
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
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. HAMAP MF_00156

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. HAMAP MF_00156

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. HAMAP MF_00156

Subcellular location

Cytoplasm Potential HAMAP MF_00156.

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2572573-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000184806

Regions

Region44 – 452Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding441Magnesium By similarity
Metal binding821Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site821Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YWS8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 69A0949DDC7064C1

FASTA25727,896
        10         20         30         40         50         60 
MPVTTQQLIQ WKQQGRSIVA LTAWDYTIAQ ILDGAGVDLI LVGDSMAVML GYKTTLPITL 

        70         80         90        100        110        120 
EEMLHHAKAV CRGVQRALVV VDLPFLTYQE SIPQAINSAG RILKETGAQA VKLEGGYPAM 

       130        140        150        160        170        180 
VDTINRLVQA GIPVMGHVGL TPQSVHQLGL RQQGKTQETA QRILNEAIAL EQAGVFSIVL 

       190        200        210        220        230        240 
EHIPADLAMQ ITQKVNIPTI GIGAGSHCDG QVLVTSDVLG LSERQPPFAK VYTNLRETIT 

       250 
KAVQDYAAEV RDRQFPE 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB77888.1.
PIRAD1996.
RefSeqNP_485562.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YWS8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YWS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1105114.
GenomeReviewsGene locus all1522 in contig BA000019_GR.
KEGGana:all1522.
NMPDRfig|103690.1.peg.1829.
PATRIC22773050. VBINosSp37423_2008.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMADPIVMLT.
PhylomeDBQ8YWS8.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycNSP103690:ALL1522-MONOMER.

Family and domain databases

HAMAPMF_00156. PanB.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK00606.
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR00222. PanB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB_NOSS1
AccessionPrimary (citable) accession number: Q8YWS8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families