P0A5I0 (ISPH1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

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

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.
Sequence caution	The sequence AAK45398.1 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	isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway Inferred from electronic annotation. Source: InterPro
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: EC 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 – 335	335	4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1 HAMAP MF_00191		PRO_0000128841

Sequences

	Sequence		Length	Mass (Da)
	P0A5I0 [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. NC_002755.2. YP_177788.1. NC_000962.2.
3D structure databases
ProteinModelPortal	P0A5I0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000003988; EBMYCP00000003988; EBMYCG00000003986. EBMYCT00000071593; EBMYCP00000069652; EBMYCG00000071588.
GeneID	885830. 925400.
GenomeReviews	Gene locus MT1141 in contig AE000516_GR. Gene locus Rv1110 in contig AL123456_GR.
KEGG	mtc:MT1141. mtu:Rv1110.
PATRIC	18124272. VBIMycTub22151_1256.
TIGR	MT1141.
Organism-specific databases
TubercuList	Rv1110.
Phylogenomic databases
GeneTree	EBGT00050000016858.
HOGENOM	HBG335228.
OMA	AMAPECD.
PhylomeDB	P0A5I0.
ProtClustDB	PRK01045.
Family and domain databases
HAMAP	MF_00191. IspH. [Tree]
InterPro	IPR003451. LytB. [Graphical view]
KO	K03527.
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:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program