Q6F854 (PANB_ACIAD) 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:	ACIAD3061

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	269 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.
Sequence caution	The sequence CAG69761.1 differs from that shown. Reason: Erroneous initiation.

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 – 269	269	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297208
Regions
	Region	43 – 44	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	179	1	Proton acceptor By similarity
	Metal binding	43	1	Magnesium By similarity
	Metal binding	82	1	Magnesium By similarity
	Metal binding	112	1	Magnesium By similarity
	Binding site	82	1	Alpha-ketoisovalerate By similarity
	Binding site	110	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6F854 [UniParc]. Last modified July 24, 2007. Version 2. Checksum: A14565F768CFCC57	FASTA	269	29,111
	10 20 30 40 50 60 MISLSDLRKF KTEGRKFSCL TCYDASMAKA MEFAEIDSIL IGDSLGMVIQ GHDSTLPVTV 70 80 90 100 110 120 DDMAYHTAAV RRGNQHSFIM TDLPFMSYAT LPDALNNAKK VMQAGAQMIK IEGGAWLSES 130 140 150 160 170 180 IRVLTQNGIP VCVHLGLTPQ SVHVFGGYKL QAKTREAADQ LIADCQAVVD AGAAILLLEC 190 200 210 220 230 240 VPAQLGQEIA ELFPQTPVIG IGAGKETDGQ VLVAQDMLGL SFGKVARFVR NFMKEQAGET 250 260 AIVDAFKAYH AAVQDQSFPA REHTFQVEL

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ADP1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG69761.1. Different initiation.
RefSeq	YP_047583.1. NC_005966.1.
3D structure databases
HSSP	HSSP built from PDB template 1M3U based on UniProtKB P31057.
ProteinModelPortal	Q6F854.
SMR	Q6F854. Positions 2-266.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6F854.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2880497.
GenomeReviews	Gene locus ACIAD3061 in contig CR543861_GR.
KEGG	aci:ACIAD3061.
NMPDR	fig|62977.3.peg.2776.
PATRIC	20743623. VBIAciSp98416_2735.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	YDATFAH.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD3061-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_ACIAD

Accession

Primary (citable) accession number: Q6F854

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 24, 2007
Last modified:	January 25, 2012
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program