Reviewed, UniProtKB/Swiss-Prot Q9X712 (PANB_CORGL)

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:	Cgl0114, cg0149

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate. Ref.1
Catalytic activity	5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. Ref.1
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 – 269	269	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000184838
Regions
	Region	50 – 51	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	50	1	Magnesium By similarity
	Metal binding	89	1	Magnesium By similarity
	Metal binding	121	1	Magnesium By similarity
	Binding site	89	1	Alpha-ketoisovalerate By similarity
	Binding site	119	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X712-1 [UniParc]. Last modified April 23, 2003. Version 2. Checksum: C494D4FF3D2A0047	FASTA	269	28,324
	10 20 30 40 50 60 MSGIDAKKIR TRHFREAKVN GQKVSVLTSY DALSARIFDE AGVDMLLVGD SAANVVLGRD 70 80 90 100 110 120 TTLSITLDEM IVLAKAVTIA TKRALVVVDL PFGTYEVSPN QAVESAIRVM RETGAAAVKI 130 140 150 160 170 180 EGGVEIAQTI RRIVDAGIPV VGHIGYTPQS EHSLGGHVVQ GRGASSGKLI ADARALEQAG 190 200 210 220 230 240 AFAVVLEMVP AEAAREVTED LSITTIGIGA GNGTDGQVLV WQDAFGLNRG KKPRFVREYA 250 260 TLGDSLHDAA QAYIADIHAG TFPGEAESF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"D-pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction." Eggeling L., Sahm H. Appl. Environ. Microbiol. 65:1973-1979(1999) [PubMed: 10223988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X96580 Genomic DNA. Translation: CAA65397.1. Different initiation. BA000036 Genomic DNA. Translation: BAB97507.1. Different initiation. BX927148 Genomic DNA. Translation: CAF18682.1. Different initiation.
PIR	T47119.
RefSeq	NP_599367.1. YP_224411.1.
3D structure databases
SMR	Q9X712. Positions 7-266.
ModBase	Search...
Genome annotation databases
GeneID	1021087. 3345597.
GenomeReviews	Gene locus Cgl0114 in contig BA000036_GR.
KEGG	cgb:cg0149. cgl:NCgl0113.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YATPEQT.
PhylomeDB	Q9X712.
Enzyme and pathway databases
BioCyc	CGLU196627:CG0149-MONOMER.
BRENDA	2.1.2.11. 812.
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_CORGL

Accession

Primary (citable) accession number: Q9X712

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	April 23, 2003
Last modified:	February 9, 2010
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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