Q5PBP6 (PANB_ANAMM) 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:	AM142

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	277 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 – 277	277	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297215
Regions
	Region	42 – 43	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	179	1	Proton acceptor By similarity
	Metal binding	42	1	Magnesium By similarity
	Metal binding	81	1	Magnesium By similarity
	Metal binding	112	1	Magnesium By similarity
	Binding site	81	1	Alpha-ketoisovalerate By similarity
	Binding site	110	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PBP6 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 001FF628D4F0FBAD	FASTA	277	30,012
	10 20 30 40 50 60 MLLNILDIQA KKGLEKIACL TAYTFPMARI LDEHCDLILV GDSVGQTVYG MESTLSVTLD 70 80 90 100 110 120 MMIAHGKAVV KARSKALVVV DMPFASYYTP ELAYKNASRI LSETGCDAVK LEGGVCVAEE 130 140 150 160 170 180 IAFLVARGIP VMGHVGLMPQ HFNQLGGYKC QGKTDSSRQH IKEDAKAVCE AGAFCVVLEC 190 200 210 220 230 240 ISPSLAAELT QELPVPTIGI GASNACDGQI LVVDDMLGQS SRYPKFVKRF ADLEHTIKDA 250 260 270 VVGYVRAVKC SEFPGDEHCY SDGPHLRVFR AHPHHAQ

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86283.1.
RefSeq	YP_153538.1. NC_004842.2.
3D structure databases
HSSP	HSSP built from PDB template 1OY0 based on UniProtKB P0A5Q8.
ProteinModelPortal	Q5PBP6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PBP6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171037.
GenomeReviews	Gene locus AM142 in contig CP000030_GR.
KEGG	ama:AM142.
PATRIC	20946379. VBIAnaMar46146_0126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	MAHVGLM.
PhylomeDB	Q5PBP6.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	AMAR234826:AM142-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_ANAMM

Accession

Primary (citable) accession number: Q5PBP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program