Reviewed, UniProtKB/Swiss-Prot Q1IHA5 (PANB_ACIBL)

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:	Acid345_4746

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	295 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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding 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 – 295	295	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297204
Regions
	Region	53 – 54	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	191	1	Proton acceptor By similarity
	Metal binding	53	1	Magnesium By similarity
	Metal binding	92	1	Magnesium By similarity
	Metal binding	124	1	Magnesium By similarity
	Binding site	92	1	Alpha-ketoisovalerate By similarity
	Binding site	122	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IHA5-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 35690AD3B63C3C84	FASTA	295	32,173
	10 20 30 40 50 60 MSIATGDFRS KVTSSTLLDK KSKHDPITCL TAYDYSTARL VDEAGIDMIL VGDSLAQTML 70 80 90 100 110 120 GYENTLPVTM DEMLHHTRAV RRAVRHAFLI ADMPYASYHV GGRESVRNAA RFIKEGGAEA 130 140 150 160 170 180 VKIEGGENRA ALIDRLLDAE VPVVGHIGLT PQSVHRMGGY KVQGKTIRDI EQLMRDATAL 190 200 210 220 230 240 DRAGVVALVL EGIPREVAAM ITAEVETPTI GIGAGPDCDG QVLVFHDILN LTFAPPAKFV 250 260 270 280 290 RRYADAAELI TGAVKAFRDD VKTGSYPSDD ESYHLPKEAQ ATLEMVQNRK HAMRK

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF43745.1.
RefSeq	YP_593819.1.
3D structure databases
SMR	Q1IHA5. Positions 12-274.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IHA5.
Genome annotation databases
GeneID	4070684.
GenomeReviews	Gene locus Acid345_4746 in contig CP000360_GR.
KEGG	aba:Acid345_4746.
NMPDR	fig|204669.6.peg.4723.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	YATPEQT.
PhylomeDB	Q1IHA5.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_4746-MONOMER.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [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.
TIGRFAMs	TIGR00222. panB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB_ACIBL

Accession

Primary (citable) accession number: Q1IHA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	June 13, 2006
Last modified:	February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)