B0V5M5 (PANB_ACIBY) 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:	ABAYE3175

Organism

Acinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]

Taxonomic identifier

509173 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

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.

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_1000096935
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)
	B0V5M5 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: A92CEDA056752238	FASTA	269	28,976
	10 20 30 40 50 60 MISLSDLRKF KAEGRKFSCL TCYDASMAKA MELAEIDTIL IGDSLGMAIQ GRDSTLPVTV 70 80 90 100 110 120 EDMAYHTAAV RRGNQHALIM TDLPFMSYAT LNDALQNAKT VMQAGAQMIK IEGGAWLSET 130 140 150 160 170 180 VQVLTRNGVP VCVHLGLTPQ SVHVFGGYKL QARTREAADQ LIADCTAVVE AGAAVLLLEC 190 200 210 220 230 240 VPAQLGQEIA ELFPNTPVIG IGAGNATDGQ VLVVQDMLGL TFGRVARFVR NFMKEQSGET 250 260 AILDAFKAFH AAVQDQSFPA KEHTFQVEL

References

[1]

"Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AYE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU459141 Genomic DNA. Translation: CAM87984.1.
RefSeq	YP_001714956.1. NC_010410.1.
3D structure databases
ProteinModelPortal	B0V5M5.
SMR	B0V5M5. Positions 2-266.
ModBase	Search...
Protein-protein interaction databases
STRING	B0V5M5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6003606.
GenomeReviews	Gene locus ABAYE3175 in contig CU459141_GR.
PATRIC	20729518. VBIAciBau69881_3056.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YDATFAH.
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.
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_ACIBY

Accession

Primary (citable) accession number: B0V5M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program