Q9JZW6 (PANB_NEIMB) 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:	NMB0870

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	263 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 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 Probable. Ref.2
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	3D-structure Complete proteome Reference 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 – 263

263

3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156

PRO_0000184867

Regions

Region

43 – 44

2

Alpha-ketoisovalerate binding HAMAP MF_00156

Sites

Active site

179

1

Proton acceptor By similarity

Metal binding

43

1

Magnesium By similarity

Metal binding

82

1

Magnesium By similarity

Metal binding

113

1

Magnesium By similarity

Binding site

82

1

Alpha-ketoisovalerate

Binding site

111

1

Alpha-ketoisovalerate

Secondary structure

1

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263

Helix Strand Turn

Details...

Helix

4 – 13

10

Beta strand

17 – 21

5

Helix

25 – 33

9

Beta strand

38 – 41

4

Helix

45 – 48

4

Beta strand

53 – 55

3

Helix

60 – 73

14

Beta strand

75 – 82

8

Beta strand

87 – 90

4

Helix

92 – 104

13

Beta strand

108 – 113

6

Helix

116 – 118

3

Helix

119 – 127

9

Beta strand

132 – 138

7

Helix

140 – 142

3

Helix

158 – 170

13

Beta strand

174 – 180

7

Helix

183 – 192

10

Beta strand

197 – 202

6

Beta strand

206 – 211

6

Helix

213 – 216

4

Beta strand

220 – 223

4

Helix

238 – 250

13

Helix

257 – 259

3

Sequences

	Sequence		Length	Mass (Da)
	Q9JZW6 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B863D8238F320317	FASTA	263	27,739
	10 20 30 40 50 60 MITVNTLQKM KAAGEKIAML TAYESSFAAL MDDAGVEMLL VGDSLGMAVQ GRKSTLPVSL 70 80 90 100 110 120 RDMCYHTECV ARGAKNAMIV SDLPFGAYQQ SKEQAFAAAA ELMAAGAHMV KLEGGVWMAE 130 140 150 160 170 180 TTEFLQMRGI PVCAHIGLTP QSVFAFGGYK VQGRGGKAQA LLNDAKAHDD AGAAVVLMEC 190 200 210 220 230 240 VLAELAKKVT ETVSCPTIGI GAGADCDGQV LVMHDMLGIF PGKTAKFVKN FMQGHDSVQA 250 260 AVRAYVAEVK AKTFPAAEHI FAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.
[2]	"Structural analysis of a set of proteins resulting from a bacterial genomics project." Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D., Hendle J. , Huber A., Hoda K., Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R. Proteins 60:787-796(2005) [PubMed: 16021622] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-263 IN COMPLEX WITH SUBSTRATE AND SODIUM ION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE002098 Genomic DNA. Translation: AAF41281.1.

PIR

F81148.

RefSeq

NP_273911.1. NC_003112.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O66	X-ray	1.75	A/B/C/D/E	2-263	[»]
1O68	X-ray	2.10	A/B/C/D/E	2-263	[»]

ProteinModelPortal

Q9JZW6.

SMR

Q9JZW6. Positions 1-261.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBNEIT00000009893; EBNEIP00000009513; EBNEIG00000009893.

GeneID

902986.

GenomeReviews

Gene locus NMB0870 in contig AE002098_GR.

KEGG

nme:NMB0870.

NMPDR

fig|122586.1.peg.845.

PATRIC

20357133. VBINeiMen85645_1083.

TIGR

NMB0870.

Phylogenomic databases

GeneTree

EBGT00050000020443.

HOGENOM

HBG299908.

OMA

YDATFAH.

ProtClustDB

PRK00311.

Enzyme and pathway databases

BioCyc

NMEN122586:NMB_0870-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_NEIMB

Accession

Primary (citable) accession number: Q9JZW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program