4-hydroxy-3-methylbut-2-enyl diphosphate reductase - Synechocystis sp. (strain PCC 6803 / Kazusa)

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Q55643 (ISPH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	slr0348

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP-Rule MF_00191 Dimethylallyl diphosphate + NAD(P)⁺ + H₂O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP-Rule MF_00191
Cofactor	Binds 1 3Fe-4S cluster per subunit By similarity.
Pathway	Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. Ref.4 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. Ref.4
Sequence similarities	Belongs to the IspH family.
Sequence caution	The sequence BAA10159.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	3Fe-4S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	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 – 379

379

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

PRO_0000128880

Regions

Region

290 – 292

Substrate binding By similarity

Sites

Metal binding

Iron-sulfur (3Fe-4S) By similarity

Metal binding

130

Iron-sulfur (3Fe-4S) By similarity

Metal binding

261

Iron-sulfur (3Fe-4S) By similarity

Binding site

Substrate By similarity

Binding site

108

Substrate By similarity

Binding site

158

Substrate By similarity

Binding site

223

Substrate By similarity

Binding site

352

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q55643 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 4CD0167AF5D4957E
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FASTA

379

42,415

        10         20         30         40         50         60 
MGVMNTEYQS HLIQEIRQNN YRLERGDVTI LLAEAFGFCW GVERAVAMAY ETRQHFPGDR 

        70         80         90        100        110        120 
LWITNEIIHN PSVNQRLREM EVNFIDVVNG EKDFSGVAKG DVVILPAFGA SVEEMQLLND 

       130        140        150        160        170        180 
RECTIVDTTC PWVSKVWNSV EKHKKKEHTS IIHGKYNHEE TIATSSFAGT YLIVLNMAEA 

       190        200        210        220        230        240 
QKVCDYILHG GDRQEFLDYF ANAHSAGFDP DQDLVRLGVA NQTTMLKSET EMIGKLFEKT 

       250        260        270        280        290        300 
LLQKYGPIEL NNHFMSFNTI CDATQERQDA MFDLVEEDLS LMVVIGGFNS SNTTHLQEIA 

       310        320        330        340        350        360 
VEHGIPSVHI DSGDRIGPGN RVEHKPLGKD LEVLEPWLPA GKITVGVTSG ASTPDKVVEE 

       370 
VMKKILAIKE AQPVLEIAG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three insertion sequences from the cyanobacterium Synechocystis PCC6803 support the occurrence of horizontal DNA transfer among bacteria." Cassier-Chauvat C., Poncelet M., Chauvat F. Gene 195:257-266(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
[3]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[4]	"Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis." Cunningham F.X. Jr., Lafond T.P., Gantt E. J. Bacteriol. 182:5841-5848(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PATHWAY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U38915 Genomic DNA. Translation: AAB72119.1. BA000022 Genomic DNA. Translation: BAA10159.1. Different initiation.
PIR	S76307.
RefSeq	NP_442089.1. NC_000911.1. YP_005652147.1. NC_017277.1. YP_007451966.1. NC_020286.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q55643. 4 interactions.
STRING	1148.slr0348.
Proteomic databases
PaxDb	Q55643.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA10159; BAA10159; BAA10159.
GeneID	12253360. 14617636. 952940.
KEGG	syn:slr0348. syy:SYNGTS_2194.
PATRIC	23841772. VBISynSp132158_2433.
Phylogenomic databases
eggNOG	COG0761.
KO	K03527.
OMA	QDAMFSL.
ProtClustDB	PRK13371.
Enzyme and pathway databases
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...

Entry information

Entry name

ISPH_SYNY3

Accession

Primary (citable) accession number: Q55643
Secondary accession number(s): Q55066

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents