Reviewed, UniProtKB/Swiss-Prot P0A5I0 (ISPH1_MYCTU)

Names and origin

Protein names

Recommended name:
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
    EC=1.17.1.2

Gene names

Name:	ispH1
Synonyms:	lytB1
Ordered Locus Names:	Rv1110, MT1141
ORF Names:	MTV017.63

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	335 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) By similarity. 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. HAMAP MF_00191 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. HAMAP MF_00191
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 – 335	335	4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1 HAMAP MF_00191		PRO_0000128841

Sequences

	Sequence		Length	Mass (Da)
	P0A5I0-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: E6640BC3246BDDBB	FASTA	335	36,297
	10 20 30 40 50 60 MVPTVDMGIP GASVSSRSVA DRPNRKRVLL AEPRGYCAGV DRAVETVERA LQKHGPPVYV 70 80 90 100 110 120 RHEIVHNRHV VDTLAKAGAV FVEETEQVPE GAIVVFSAHG VAPTVHVSAS ERNLQVIDAT 130 140 150 160 170 180 CPLVTKVHNE ARRFARDDYD ILLIGHEGHE EVVGTAGEAP DHVQLVDGVD AVDQVTVRDE 190 200 210 220 230 240 DKVVWLSQTT LSVDETMEIV GRLRRRFPKL QDPPSDDICY ATQNRQVAVK AMAPECELVI 250 260 270 280 290 300 VVGSRNSSNS VRLVEVALGA GARAAHLVDW ADDIDSAWLD GVTTVGVTSG ASVPEVLVRG 310 320 330 VLERLAECGY DIVQPVTTAN ETLVFALPRE LRSPR

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842575 Genomic DNA. Translation: CAE55361.1. AE000516 Genomic DNA. Translation: AAK45398.1. Different initiation.
PIR	D70898.
RefSeq	NP_335584.1. YP_177788.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	885830. 925400.
GenomeReviews	Gene locus MT1141 in contig AE000516_GR.
KEGG	mtc:MT1141. mtu:Rv1110.
TIGR	MT1141.
Organism-specific databases
TubercuList	Rv1110.
Phylogenomic databases
HOGENOM	HBG335228.
OMA	HMQVARA.
Enzyme and pathway databases
BRENDA	1.17.1.2. 809.
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

ISPH1_MYCTU

Accession

Primary (citable) accession number: P0A5I0
Secondary accession number(s): O53458

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)