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A1US40 (PANB_BARBK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BARBAKC583_0477
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length271 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 – 2712713-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000297223

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
A1US40 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 8959EE2FC25A1CE7

FASTA27129,423
        10         20         30         40         50         60 
MSVHKSIKRI TASEIQAKKK QEPIVSLTAY QAYSARIADP HCDFLLVGDS VGMIVHGFDT 

        70         80         90        100        110        120 
TLPVDVDMMI LHGKAVMRGS QRALVVVDMP FGSYEKSPEQ AFSNASRILA DTGCGAVKLE 

       130        140        150        160        170        180 
GGIHMAKTID FLCKRGIPVM SHIGLTPQAV NHFGGFKTQG RDKSDWEKIE ADAAAIEDAG 

       190        200        210        220        230        240 
AFAVVVEAVV EPLAVKLTEK LSIPTIGIGA SNQCDGQILV MEDMLGYGAW APKFVRRYGT 

       250        260        270 
LEQAMDTAIR NYAEDVKSRA FPSDSEIYKL K 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35685 / KC583.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000524 Genomic DNA. Translation: ABM44890.1.
RefSeqYP_988793.1. NC_008783.1.

3D structure databases

ProteinModelPortalA1US40.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1US40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4684397.
GenomeReviewsGene locus BARBAKC583_0477 in contig CP000524_GR.
KEGGbbk:BARBAKC583_0477.
NMPDRfig|360095.3.peg.170.
PATRIC20537223. VBIBarBac6912_0459.
TIGRBARBAKC583_0477.

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMADPIVMLT.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycBBAC360095:BARBAKC583_0477-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_BARBK
AccessionPrimary (citable) accession number: A1US40
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 38 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