Q9PIK1 (PANB_CAMJE) 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:	Cj0298c

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	274 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 – 274	274	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184832
Regions
	Region	44 – 45	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	182	1	Proton acceptor By similarity
	Metal binding	44	1	Magnesium By similarity
	Metal binding	83	1	Magnesium By similarity
	Metal binding	115	1	Magnesium By similarity
	Binding site	83	1	Alpha-ketoisovalerate By similarity
	Binding site	113	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PIK1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 9B3CACB32EFDE0C7	FASTA	274	30,202
	10 20 30 40 50 60 MRKSMISFLE KKAKNEKITM VSAYDYHSAR ILDNSDIDII LVGDSLAMTV LGMQDTLSVT 70 80 90 100 110 120 MDEMLIFTKA VSRGAKKSFV LADMPFMSYQ SSDRDAILNA SRFIKESHAN GVKVEGGIEI 130 140 150 160 170 180 ASKIKLISQS GIPVVAHLGL TPQAVNMLGG YRVQGKDLQS AQKIIDDAKA VQDAGACMLV 190 200 210 220 230 240 LECVPVKLAQ KISSILEIPT IGIGSGKYCD GQVLVYHDLL GLNKDFKAKF VKHFDKIDPQ 250 260 270 VGVEKYRDEV KSGIFPSQEH SFDYLDDELL DKLY

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34449.1.
PIR	F81448.
RefSeq	YP_002343736.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PIK1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	904622.
GenomeReviews	Gene locus Cj0298c in contig AL111168_GR.
KEGG	cje:Cj0298c.
PATRIC	20057513. VBICamJej33762_0290.
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YDATFAH.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0298C-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_CAMJE

Accession

Primary (citable) accession number: Q9PIK1
Secondary accession number(s): Q0PBL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program