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A6TMH9 (PANB_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 32. 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:Amet_1189
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length282 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 – 2822823-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000058180

Regions

Region46 – 472Alpha-ketoisovalerate binding By similarity

Sites

Active site1841Proton acceptor By similarity
Metal binding461Magnesium By similarity
Metal binding851Magnesium By similarity
Metal binding1171Magnesium By similarity
Binding site851Alpha-ketoisovalerate By similarity
Binding site1151Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A6TMH9 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: EF7083A3CA74F998

FASTA28230,924
        10         20         30         40         50         60 
MAKKKSILDL MKMKKAEEQV AWVTAYDFPT ASFAEQAGME MILVGDSLGM VVLGYQGTIP 

        70         80         90        100        110        120 
VTMEDCISHC QAVRRGAPNT WVIGDMPFGS YQVSDEDAVR NAVRFMKEAD VDCIKLEGGD 

       130        140        150        160        170        180 
RVKSRIRAIT DAGIPVMGHI GLTPQSSGQL GGFKAQGRRV DNARVLIQDA LVVQEAGAFS 

       190        200        210        220        230        240 
LLVEAVPPEV TKFIADKLDI PVYSIGAGPC DGQLVISGDM LGKFQAFTPK FIKKYANVAE 

       250        260        270        280 
VETNAFKEYV AEVKAGQFPT DDHVYHILDT QEEFEKLFQE FK 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR47397.1.
RefSeqYP_001319056.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TMH9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6TMH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5311240.
GenomeReviewsGene locus Amet_1189 in contig CP000724_GR.
KEGGamt:Amet_1189.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAPENTINM.
ProtClustDBCLSK2792147.

Enzyme and pathway databases

BioCycAMET293826:AMET_1189-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_ALKMQ
AccessionPrimary (citable) accession number: A6TMH9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: November 16, 2011
This is version 32 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