A1TTV9 (PANB_ACIAC) 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:	Aave_3852

Organism

Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]

Taxonomic identifier

397945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	296 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 – 296	296	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_0000297206
Regions
	Region	71 – 72	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	212	1	Proton acceptor By similarity
	Metal binding	71	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Metal binding	145	1	Magnesium By similarity
	Binding site	114	1	Alpha-ketoisovalerate By similarity
	Binding site	143	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1TTV9 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: F6DEA9EA88BF4064	FASTA	296	30,857
	10 20 30 40 50 60 MTAPTPTPAN AATPYGTLPP ASPLPQRRPV SLPRLAQMRE AGEKITMLTA YDATFAAVAD 70 80 90 100 110 120 AAGVECLLVG DSLGMVCQGL PSTVGVSLDT MAYHTASVAR GLHRVQGTAW LIADLPYGSY 130 140 150 160 170 180 AEGPEQAMRS ACTLMQAGAH MVKLEGGGWT APTVRFLVER GVPVCAHLGL TPQTVHALGG 190 200 210 220 230 240 YRVQGRSDEA ARALRSQANE LQDAGAAMLV LEMVPATLAR EVTDALPRCH TIGIGAGSGT 250 260 270 280 290 AGQVLVLHDM LGVNLGKNPK FAHDFMAQAG SVRGAIEAYV QAVKAGRFPD DALHAW

References

[1]

"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AAC00-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000512 Genomic DNA. Translation: ABM34397.1.
RefSeq	YP_972171.1. NC_008752.1.
3D structure databases
ProteinModelPortal	A1TTV9.
SMR	A1TTV9. Positions 30-292.
ModBase	Search...
Protein-protein interaction databases
STRING	A1TTV9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4667381.
GenomeReviews	Gene locus Aave_3852 in contig CP000512_GR.
KEGG	aav:Aave_3852.
PATRIC	20682869. VBIAciCit38535_3900.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0413.
HOGENOM	HBG299908.
OMA	YDATFAH.
PhylomeDB	A1TTV9.
ProtClustDB	PRK00311.
Enzyme and pathway databases
BioCyc	AAVE397945:AAVE_3852-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_ACIAC

Accession

Primary (citable) accession number: A1TTV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program