Reviewed, UniProtKB/Swiss-Prot Q7W3E7 (PANB_BORPA)

Names and origin

Protein names

Recommended 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:	BPP4094

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
Subcellular location	Cytoplasm Potential.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding 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 – 278	278	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184822
Regions
	Region	49 – 50	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	186	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)
	Q7W3E7-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 483FD1875CC7850F	FASTA	278	29,189
	10 20 30 40 50 60 MSVPTAAKRI TTRQLRMRTP DEPIVALTAY TAPIAGLLDA HCDLLLVGDS LGMVIYGMET 70 80 90 100 110 120 TLPVTVDMMI QHGRAVMRGS QRACVAVDMP FGSYQEDERQ AYRNAARIMA ETGASCVKLE 130 140 150 160 170 180 GGAEMASTVA FLVERGIPVM GHVGLKPQSV HGHGGFRTVG RGAEAEQVMA DAQAIAAAGA 190 200 210 220 230 240 FTVVIEGTLE PVARAITEAL PVPTIGIGAS PACGGQILVS DDVLGLFSDF TPRFVKRYAQ 250 260 270 LGPIIEQAAA AYASEVRART FPAPEHCTGM PAPDGRPA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640435 Genomic DNA. Translation: CAE39375.1.
RefSeq	NP_886232.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1667606.
GenomeReviews	Gene locus BPP4094 in contig BX470249_GR.
KEGG	bpa:BPP4094.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W3E7.
OMA	LVVVDMP.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4094-MON.
BRENDA	2.1.2.11. 263123.
Family and domain databases
HAMAP	MF_00156. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHER	PTHR20881. Pantoate_transf. 1 hit.
Pfam	PF02548. Pantoate_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
TIGRFAMs	TIGR00222. panB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB_BORPA

Accession

Primary (citable) accession number: Q7W3E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)