Reviewed, UniProtKB/Swiss-Prot P65655 (PANB_BRUSU)

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:	BR0330

Organism

Brucella suis [Complete proteome] [HAMAP]

Taxonomic identifier

29461 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	275 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 – 275	275	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184827
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)
	P65655-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: F73117B84258FE26	FASTA	275	29,418
	10 20 30 40 50 60 MSAPVTRKRL TPKVIQAMKG ECPIVSLTAY TTPVARLLDP HCDLLLVGDS LGMVLYGMES 70 80 90 100 110 120 TLAVTLDMMI MHGQAVMRGT SHACVIVDMP FGSYQESKEQ AFRNAARVMQ ETGCDGVKLE 130 140 150 160 170 180 GGEEMAETVA FLVRRGIPVF GHVGLMPQQV NTVGGFRSLG RGDDEAGKIR RDAQAIAQAG 190 200 210 220 230 240 AFAVVIEGTV EPLAREITAL IDIPTVGIGA SSACDGQVLV SDDMLGLFQD FTPRFVKRFA 250 260 270 HLAPQVSQAA EAYAEEVRAR RFPGPEHVFG AKPGA

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330 / Biovar 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014291 Genomic DNA. Translation: AAN29279.1.
RefSeq	NP_697364.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1165991.
GenomeReviews	Gene locus BR0330 in contig AE014291_GR.
KEGG	bms:BR0330.
TIGR	BR0330.
Phylogenomic databases
HOGENOM	P65655.
OMA	DMMIAHG
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0330-MON.
BRENDA	2.1.2.11. 281610.
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_BRUSU

Accession

Primary (citable) accession number: P65655
Secondary accession number(s): Q8YFD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 24, 2009
This is version 33 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)