Reviewed, UniProtKB/Swiss-Prot Q8UA91 (PANB_AGRT5)

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:	Atu3483
ORF Names:	AGR_L_2695

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
Subcellular location	Cytoplasm Potential.
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 – 279	279	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184805
Regions
	Region	49 – 50	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	49	1	Magnesium By similarity
	Metal binding	88	1	Magnesium By similarity
	Metal binding	120	1	Magnesium By similarity
	Binding site	88	1	Alpha-ketoisovalerate By similarity
	Binding site	118	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8UA91-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 429B3D572C467678	FASTA	279	29,759
	10 20 30 40 50 60 MSAHAKQKRL TTASIRQMKG EARIVCLTAY TTPIARLLDP HCDLLLVGDS LGMVLYGMET 70 80 90 100 110 120 TVGVTLDMMI AHGRAVMRGV EHACVIVDLP FGTYQESKEQ AFRNAVRLMQ ETGCDGVKLE 130 140 150 160 170 180 GGEEMAETIA FLVARGIPVF GHVGLMPQLV HTAGGFRSLG HSDAETQKIW RDGIAVDQAG 190 200 210 220 230 240 AFAIVVEGTV EPLARELTEK LAAPTVGIGA SPACDGQVLV SDDMLGLFSD FKPKFVKRYA 250 260 270 DLGTAATQAA AAYADEVRSG AFPGPEHTFQ VRKPSPSGK

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE007870 Genomic DNA. Translation: AAK89911.1.
PIR	AB2985. E98298.
RefSeq	NP_357126.1.
3D structure databases
HSSP	HSSP built from PDB template 1OY0 based on UniProtKB Q10505.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UA91.
Genome annotation databases
GeneID	1135357.
GenomeReviews	Gene locus Atu3483 in contig AE007870_GR.
KEGG	atc:AGR_L_2695. atu:Atu3483.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8UA91.
OMA	LVVVDMP.
Family and domain databases
HAMAP	MF_00156. [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_AGRT5

Accession

Primary (citable) accession number: Q8UA91

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 43 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)