Q0B4Z6 (PANB2_BURCM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Bamb_5229

Organism

Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]

Taxonomic identifier

339670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 284	284	3-methyl-2-oxobutanoate hydroxymethyltransferase 2 HAMAP MF_00156		PRO_0000297232
Regions
	Region	49 – 50	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	49	1	Magnesium By similarity
	Metal binding	88	1	Magnesium By similarity
	Metal binding	120	1	Magnesium By similarity
	Binding site	88	1	Alpha-ketoisovalerate By similarity
	Binding site	118	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0B4Z6 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 042652B4D6D3BF68	FASTA	284	29,849
	10 20 30 40 50 60 MSAHTRITRK TVTAIRSTKG IGSLVSLTAY SAPMAKLVHD VADVIIVGDS VGMVLYGMPD 70 80 90 100 110 120 TLRVTLDMMI AHGAAVVRGA AQACVVVDLP FSTFQESPAQ AYRSAARLLA ETGAQAVKLE 130 140 150 160 170 180 GGCEMTDTIR FLTERGIPVM AHVGLMPQQA NAAGGFRAQG MDPLSAAQVF DAACAAERAG 190 200 210 220 230 240 AFSVVIEGTA EALARHLTGT LTIPTIGIGA SPACDGQVLV TEDMIGAFDA YTPRFVKRYA 250 260 270 280 DANAVMRDAI RQYAHDVRHR VFPEPAHCFG YGKPLQLADA GATV

References

[1]

"Complete sequence of chromosome 2 of Burkholderia cepacia AMMD." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000441 Genomic DNA. Translation: ABI90777.1.
RefSeq	YP_777111.1. NC_008391.1.
3D structure databases
ProteinModelPortal	Q0B4Z6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0B4Z6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4314119.
GenomeReviews	Gene locus Bamb_5229 in contig CP000441_GR.
KEGG	bam:Bamb_5229.
NMPDR	fig|339670.3.peg.1478.
PATRIC	19026451. VBIBurAmb61564_5476.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	MAHVGLM.
ProtClustDB	CLSK770141.
Enzyme and pathway databases
BioCyc	BAMB339670:BAMB_5229-MONOMER.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K00606.
PANTHER	PTHR20881. Pantoate_transf. 1 hit.
Pfam	PF02548. Pantoate_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR00222. PanB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB2_BURCM

Accession

Primary (citable) accession number: Q0B4Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program