Reviewed, UniProtKB/Swiss-Prot Q5NL34 (PANB1_ZYMMO)

Names and origin

Protein names

Recommended name:
    3-methyl-2-oxobutanoate hydroxymethyltransferase 1
    EC=2.1.2.11
Alternative name(s):
    Ketopantoate hydroxymethyltransferase 1
      Short name=KPHMT 1

Gene names

Name:	panB1
Ordered Locus Names:	ZMO1952

Organism

Zymomonas mobilis [Complete proteome] [HAMAP]

Taxonomic identifier

542 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas

Protein attributes

Sequence length	302 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 – 302	302	3-methyl-2-oxobutanoate hydroxymethyltransferase 1 HAMAP MF_00156		PRO_0000297418
Regions
	Region	75 – 76	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	217	1	Proton acceptor By similarity
	Metal binding	75	1	Magnesium By similarity
	Metal binding	118	1	Magnesium By similarity
	Metal binding	149	1	Magnesium By similarity
	Binding site	118	1	Alpha-ketoisovalerate By similarity
	Binding site	147	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5NL34-1 [UniParc]. Last modified July 24, 2007. Version 2. Checksum: 14A01F5A53B4C43D	FASTA	302	31,784
	10 20 30 40 50 60 MNQHGRSAEP GVASEGIAPY GDAHRGIAAK RKKTTTARIS QMRVDGEKIA VLTAYDATFA 70 80 90 100 110 120 AAADAAGVDC IMVGDSLGMV CQGRTTTVGV SLEDMLYHTR CVSQGIARAD GSALIIADLP 130 140 150 160 170 180 FGSYQQSNEQ AIASAVQLMQ AGAHMVKLEG GDWWTVDIVE FLVQRGIPVC AHLRLTPQTV 190 200 210 220 230 240 SALGGYRVQG RSEEAAEKLR VDAGALDNAG ASMMVLEMIP TELATSITSE MKSCATIGIG 250 260 270 280 290 300 AGSGTAGQVL VMHDMLGINL GRMAKFVRNF MRDAEDVPTA FAAYVAAVKD GSFPDDKLHG FL

References

[1]

"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008692 Genomic DNA. Translation: AAV90576.1. Different initiation.
RefSeq	YP_163687.1.
3D structure databases
HSSP	HSSP built from PDB template 1O66 based on UniProtKB Q9JZW6.
SMR	Q5NL34. Positions 35-297.
ModBase	Search...
Genome annotation databases
GeneID	3189342.
GenomeReviews	Gene locus ZMO1952 in contig AE008692_GR.
KEGG	zmo:ZMO1952.
NMPDR	fig|264203.3.peg.1364.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YHTECVV.
Enzyme and pathway databases
BioCyc	ZMOB264203:ZMO1952-MONOMER.
BRENDA	2.1.2.11. 1658.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
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

PANB1_ZYMMO

Accession

Primary (citable) accession number: Q5NL34

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 24, 2007
Last modified:	February 9, 2010
This is version 35 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)