Q98NC9 (PANB_RHILO) Reviewed, UniProtKB/Swiss-Prot

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:	mll0197

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length	286 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 – 286	286	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184880
Regions
	Region	51 – 52	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	189	1	Proton acceptor By similarity
	Metal binding	51	1	Magnesium By similarity
	Metal binding	90	1	Magnesium By similarity
	Metal binding	122	1	Magnesium By similarity
	Binding site	90	1	Alpha-ketoisovalerate By similarity
	Binding site	120	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q98NC9 [UniParc]. Last modified September 26, 2001. Version 1. Checksum: F217B148D85D7C9B	FASTA	286	29,638
	10 20 30 40 50 60 MATKLPTTDI RIGAELIRRR KGGVPLVCLT AYTYPVARLL DPHVDLLLVG DSVSMVLHGH 70 80 90 100 110 120 ATTLGASLGM MIAHGQAVMR GSARACVVVD MPAGSYEDSA AQAVASARRI VDETGCQAVK 130 140 150 160 170 180 LEGGVDMAGQ IAAIAAAGIP VMGHIGLLPQ SVEKDGGYKI KGRTDETVAA LMADARAVEK 190 200 210 220 230 240 AGAFSVVIEG TIEAVAADIT RRIAIPTIGI GASGDCDGQI LVIDDMVGLT VDRVPKFVKE 250 260 270 280 YADLRSVIAN AAERYAAEVR DRTFPGPSHV FSGSKASSDL NGGDES

References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S. DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB47832.1.
RefSeq	NP_102046.1. NC_002678.2.
3D structure databases
ProteinModelPortal	Q98NC9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1224709.
GenomeReviews	Gene locus mll0197 in contig BA000012_GR.
KEGG	mlo:mll0197.
NMPDR	fig|266835.1.peg.151.
PATRIC	22474454. VBIMesLot2464_0153.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	MAHVGLM.
ProtClustDB	PRK00311.
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

PANB_RHILO

Accession

Primary (citable) accession number: Q98NC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program