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B4RYN8 (PANB_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 29. 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:panB1
Ordered Locus Names:MADE_1017495
AND
Name:panB2
Ordered Locus Names:MADE_1018440
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas

Protein attributes

Sequence length264 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 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096938

Regions

Region45 – 462Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding451Magnesium By similarity
Metal binding841Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site841Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RYN8 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 18A9E30BEE1D8424

FASTA26428,275
        10         20         30         40         50         60 
MKKVTVSGLL KKKQAGEKIT SLTAYDASFA KMFDEQGVDA LLIGDSLGMV LQGEDDTLPV 

        70         80         90        100        110        120 
TIDDIAYHTK SVRRGTERAF VLADMPFMSY ATPEQTYANA AKLMAAGASM VKMEGGSWLC 

       130        140        150        160        170        180 
DTIKGLNLRG VPVCGHLGLT PQSVHVFGGF KVQGREASQA EKLLSEAKAL EEAGIQLLVL 

       190        200        210        220        230        240 
ECVPSSLGKA VSEALTIPVI GIGAGKDTDG QILVMHDMFG ISANYMPKFS KNYLVETGDM 

       250        260 
RKAVSKYIED VQSGAFPSPE HSFQ

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001103 Genomic DNA. Translation: AEA99623.1.
CP001103 Genomic DNA. Translation: AEA99812.1.
RefSeqYP_004428621.1. NC_011138.2.
YP_004428810.1. NC_011138.2.

3D structure databases

ProteinModelPortalB4RYN8.
SMRB4RYN8. Positions 5-264.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4RYN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10558845.
10559034.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

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.
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_ALTMD
AccessionPrimary (citable) accession number: B4RYN8
Secondary accession number(s): F2G684
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 29 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

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