Q81FN7 (PANB_BACCR) 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:	BC_1540

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	278 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 Reference 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 – 278	278	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184810
Regions
	Region	43 – 44	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	181	1	Proton acceptor By similarity
	Metal binding	43	1	Magnesium By similarity
	Metal binding	82	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Binding site	82	1	Alpha-ketoisovalerate By similarity
	Binding site	112	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81FN7 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: BFEB4A8585D516B9	FASTA	278	30,499
	10 20 30 40 50 60 MKTKTDFLKM KEQGEPITML TAYDYPSAKL AEEAEVDMIL VGDSLGMVVL GYDSTVPVTV 70 80 90 100 110 120 EDMIHHTKAV RRGAKETFIV TDMPFMSYHV SLQETMVNAR RIVQESGAHA LKVEGAGEVI 130 140 150 160 170 180 STIQYLTNAG IPVVAHLGLT PQSVGVLGGY KVQGKDAESA KKLIEDAKKC EEAGAIALVL 190 200 210 220 230 240 ECVPMQLAEL ISEQLTIPTI GIGAGQKVDG QVLVYHDLIS YGVNRVPKFV KQYTSVQEEI 250 260 270 VRGISQYVTE VKTRQFPEEK HSFTMKEEEC LSLYGGKQ

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP08520.1.
RefSeq	NP_831319.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q81FN7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81FN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000030665; EBBACP00000029871; EBBACG00000030656.
GeneID	1203889.
GenomeReviews	Gene locus BC_1540 in contig AE016877_GR.
KEGG	bce:BC1540.
PATRIC	32598814. VBIBacCer54481_1516.
Phylogenomic databases
eggNOG	COG0413.
GeneTree	EBGT00050000000505.
HOGENOM	HBG299908.
OMA	YDATFAH.
PhylomeDB	Q81FN7.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	BCER226900:BC_1540-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

PANB_BACCR

Accession

Primary (citable) accession number: Q81FN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program