O67625 (ISPH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
EC=1.17.1.2

Gene names

Name:	ispH
Synonyms:	lytB
Ordered Locus Names:	aq_1739

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). HAMAP-Rule MF_00191
Catalytic activity	Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. Ref.2 Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. Ref.2
Cofactor	Binds 1 3Fe-4S cluster per subunit. Ref.3
Enzyme regulation	Highly sensitive to dioxygen. Ref.2
Pathway	Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. HAMAP-Rule MF_00191 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. HAMAP-Rule MF_00191
Subunit structure	Homodimer. Ref.3
Sequence similarities	Belongs to the IspH family.
Biophysicochemical properties	Kinetic parameters: KM=590 µM for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate Ref.2 pH dependence: Optimum pH is 7.0-7.5. Temperature dependence: Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	3Fe-4S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dimethylallyl diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway Inferred from electronic annotation. Source: HAMAP terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Inferred from electronic annotation. Source: HAMAP metal 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 – 289

289

4-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP-Rule MF_00191

PRO_0000128766

Regions

Region

221 – 223

3

Substrate binding By similarity

Sites

Metal binding

13

1

Iron-sulfur (3Fe-4S)

Metal binding

96

1

Iron-sulfur (3Fe-4S)

Metal binding

193

1

Iron-sulfur (3Fe-4S)

Binding site

42

1

Substrate By similarity

Binding site

74

1

Substrate By similarity

Binding site

124

1

Substrate By similarity

Binding site

165

1

Substrate By similarity

Binding site

265

1

Substrate By similarity

Secondary structure

1

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289

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Helix

14 – 26

13

Turn

27 – 29

3

Beta strand

34 – 38

5

Beta strand

40 – 42

3

Helix

44 – 53

10

Beta strand

55 – 57

3

Beta strand

68 – 71

4

Helix

78 – 86

9

Beta strand

90 – 93

4

Helix

97 – 111

15

Beta strand

115 – 120

6

Helix

125 – 136

12

Beta strand

141 – 146

6

Helix

147 – 155

9

Beta strand

157 – 163

7

Helix

169 – 182

14

Beta strand

183 – 189

7

Helix

195 – 206

12

Helix

207 – 209

3

Beta strand

210 – 217

8

Helix

222 – 234

13

Beta strand

236 – 243

8

Helix

244 – 246

3

Helix

249 – 252

4

Beta strand

256 – 262

7

Helix

268 – 280

13

Sequences

	Sequence		Length	Mass (Da)
	O67625 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A9D910C41727E9F4	FASTA	289	32,104
	10 20 30 40 50 60 MVDIIIAEHA GFCFGVKRAV KLAEESLKES QGKVYTLGPI IHNPQEVNRL KNLGVFPSQG 70 80 90 100 110 120 EEFKEGDTVI IRSHGIPPEK EEALRKKGLK VIDATCPYVK AVHEAVCQLT REGYFVVLVG 130 140 150 160 170 180 EKNHPEVIGT LGYLRACNGK GIVVETLEDI GEALKHERVG IVAQTTQNEE FFKEVVGEIA 190 200 210 220 230 240 LWVKEVKVIN TICNATSLRQ ESVKKLAPEV DVMIIIGGKN SGNTRRLYYI SKELNPNTYH 250 260 270 280 IETAEELQPE WFRGVKRVGI SAGASTPDWI IEQVKSRIQE ICEGQLVSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis." Altincicek B., Duin E.C., Reichenberg A., Hedderich R., Kollas A.-K., Hintz M., Wagner S., Wiesner J., Beck E., Jomaa H. FEBS Lett. 532:437-440(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PRESENCE OF AN IRON-SULFUR CLUSTER, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway." Rekittke I., Wiesner J., Roehrich R., Demmer U., Warkentin E., Xu W., Troschke K., Hintz M., No J.H., Duin E.C., Oldfield E., Jomaa H., Ermler U. J. Am. Chem. Soc. 130:17206-17207(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S), COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC07596.1.

PIR

G70449.

RefSeq

NP_214191.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DNF	X-ray	1.65	A/B	1-289	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

224324.aq_1739.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC07596; AAC07596; aq_1739.

GeneID

1193340.

KEGG

aae:aq_1739.

PATRIC

20960466. VBIAquAeo85532_1338.

Phylogenomic databases

eggNOG

COG0761.

HOGENOM

HOG000220193.

KO

K03527.

OMA

QDAMFSL.

ProtClustDB

CLSK2299815.

Enzyme and pathway databases

BioCyc

AAEO224324:GJBH-1242-MONOMER.

UniPathway

UPA00056; UER00097.
UPA00059; UER00105.

Family and domain databases

HAMAP

MF_00191. IspH.

InterPro

IPR003451. LytB.
[Graphical view]

Pfam

PF02401. LYTB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00216. ispH_lytB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O67625.

Entry information

Entry name

ISPH_AQUAE

Accession

Primary (citable) accession number: O67625

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program