Reviewed, UniProtKB/Swiss-Prot Q55643 (ISPH_SYNY3)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › 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 MF_00191
Catalytic activity	Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191 Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191
Cofactor	Binds 1 3Fe-4S cluster By similarity. HAMAP MF_00191
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.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	3Fe-4S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Inferred from electronic annotation. Source: HAMAP iron 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 MF_00191		PRO_0000128880

Sequences

	Sequence		Length	Mass (Da)
	Q55643-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 4CD0167AF5D4957E	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

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: 9305771] [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: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 11004185] [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.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q55643. 4 interactions.
STRING	Q55643.
Genome annotation databases
GeneID	952940.
GenomeReviews	Gene locus slr0348 in contig BA000022_GR.
KEGG	syn:slr0348.
NMPDR	fig|1148.1.peg.2190.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0761.
HOGENOM	HBG286221.
OMA	REENIEF.
Enzyme and pathway databases
BioCyc	SSP1148:SLR0348-MONOMER.
Family and domain databases
HAMAP	MF_00191. IspH. [Tree]
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:	February 9, 2010
This is version 60 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)