Reviewed, UniProtKB/Swiss-Prot Q1LTN1 (PANB_BAUCH)

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:	BCI_0230

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	265 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 – 265	265	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297224
Regions
	Region	45 – 46	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	182	1	Proton acceptor By similarity
	Metal binding	45	1	Magnesium By similarity
	Metal binding	84	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Binding site	84	1	Alpha-ketoisovalerate By similarity
	Binding site	112	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LTN1-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 55D146AD5121E275	FASTA	265	28,907
	10 20 30 40 50 60 MNITTISHLR KYKQRQQKFA AITAYDAAFA SLFEQNGIQV MLVGDSLGMT IQGNDSTLPV 70 80 90 100 110 120 TLEDMIYHTR CVRRGAPYCL LIADLPFMCY ATLYQAYDNA AALMRAGANI VKLEGGGCWV 130 140 150 160 170 180 TKIVRCLTDR AVPVCCHLGL TPQSVNILGG YKIQGRDKDS ADRILSESIA LELAGAQMLV 190 200 210 220 230 240 LECVPITLSE RIADVLTIPV IGIGAGPVTD GQILVMQDIL GITGNRIPSF AKNFLTDSRD 250 260 IPTAIQLYVQ EVETGKFPAV QHYFS

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF14057.1.
RefSeq	YP_588683.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LTN1.
Genome annotation databases
GeneID	4056431.
GenomeReviews	Gene locus BCI_0230 in contig CP000238_GR.
KEGG	bci:BCI_0230.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LTN1.
OMA	YATPEQT.
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_BAUCH

Accession

Primary (citable) accession number: Q1LTN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 24 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)