Reviewed, UniProtKB/Swiss-Prot A0JVB5 (PANB_ARTS2)

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:	Arth_1591

Organism

Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]

Taxonomic identifier

290399 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	301 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 – 301	301	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297217
Regions
	Region	82 – 83	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	219	1	Proton acceptor By similarity
	Metal binding	82	1	Magnesium By similarity
	Metal binding	121	1	Magnesium By similarity
	Metal binding	153	1	Magnesium By similarity
	Binding site	121	1	Alpha-ketoisovalerate By similarity
	Binding site	151	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0JVB5-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 294B9611227E33FA	FASTA	301	31,482
	10 20 30 40 50 60 MATSNSSDSS MSAEVPAPYG NGPANAPATP SDTAKKPVAR IRTHHLQQAK DKGEHFAMLT 70 80 90 100 110 120 AYEQYTAEIF DEAGIEVLLV GDSASNNVFG NETSLPVTVD ELLPLCRAVA RSAKRALVVA 130 140 150 160 170 180 DLPFGSYEVS AEQAVATGVR FLKEGLAHAV KIEGGKFYAD TVRAMVQAGI PVMAHIGFTP 190 200 210 220 230 240 QSEHSLGGYR VQGRGDDAQR LIDDAVALAE AGAFSVLMEM VPAATAAAVD AAIAVPTVGI 250 260 270 280 290 300 GAGNTTTGQV LVWQDMAGLR GGKMAKFVKQ YADLRTSLSN AAKAYGDDVR TGQFPGPEHS F

References

[1]

"Complete sequence of chromosome 1 of Arthrobacter sp. FB24." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000454 Genomic DNA. Translation: ABK02985.1.
RefSeq	YP_831085.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0JVB5.
Genome annotation databases
GeneID	4445888.
GenomeReviews	Gene locus Arth_1591 in contig CP000454_GR.
KEGG	art:Arth_1591.
TIGR	Arth_1591.
Phylogenomic databases
OMA	YATPEQT.
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_ARTS2

Accession

Primary (citable) accession number: A0JVB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 22 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)