A0LTD0 (PANB_ACIC1) 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:	Acel_0917

Organism

Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]

Taxonomic identifier

351607 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length	271 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 – 271	271	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297205
Regions
	Region	52 – 53	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	189	1	Proton acceptor By similarity
	Metal binding	52	1	Magnesium By similarity
	Metal binding	91	1	Magnesium By similarity
	Metal binding	123	1	Magnesium By similarity
	Binding site	91	1	Alpha-ketoisovalerate By similarity
	Binding site	121	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LTD0 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: B25C38E36F7CFF5A	FASTA	271	29,007
	10 20 30 40 50 60 MSAAADVPRR VTIHDLQLRK RQHRRWAMLT CYDALTARIF EEAGIDVLLV GDSAANTVLG 70 80 90 100 110 120 YPDTLGVDVD ELLILNRAVA RAAQRALVVA DLPFGSYQIS PRQALQTAIR FVKRAGVQAV 130 140 150 160 170 180 KFEGGRRVAE HVRTVVEAGI PVMAHIGFTP QSVHALGGYR VQGRGDDAAA IRDDALALQE 190 200 210 220 230 240 AGAFAIVLEL VPAGLAAELT AALQIPTIGI GAGPDCDAQV LVWTDMAGLT PQPTPKFVKR 250 260 270 YADLRTVLHD AARAFAADVA DGRYPDAAHS Y

References

[1]

"Complete sequence of Acidothermus cellulolyticus 11B." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000481 Genomic DNA. Translation: ABK52690.1.
RefSeq	YP_872676.1. NC_008578.1.
3D structure databases
ProteinModelPortal	A0LTD0.
SMR	A0LTD0. Positions 9-269.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LTD0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4485911.
GenomeReviews	Gene locus Acel_0917 in contig CP000481_GR.
KEGG	ace:Acel_0917.
PATRIC	20672274. VBIAciCel132453_0975.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	QVLVWTD.
Enzyme and pathway databases
BioCyc	ACEL351607:ACEL_0917-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_ACIC1

Accession

Primary (citable) accession number: A0LTD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	December 12, 2006
Last modified:	December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program