P0A5I2 (ISPH2_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	ispH2
Synonyms:	lytB2
Ordered Locus Names:	Rv3382c, MT3490
ORF Names:	MTV004.40c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	329 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 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 – 329	329	4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2 HAMAP MF_00191		PRO_0000128842

Sequences

	Sequence		Length	Mass (Da)
	P0A5I2 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 00540C5C87B2AB6B	FASTA	329	34,666
	10 20 30 40 50 60 MAEVFVGPVA QGYASGEVTV LLASPRSFCA GVERAIETVK RVLDVAEGPV YVRKQIVHNT 70 80 90 100 110 120 VVVAELRDRG AVFVEDLDEI PDPPPPGAVV VFSAHGVSPA VRAGADERGL QVVDATCPLV 130 140 150 160 170 180 AKVHAEAARF AARGDTVVFI GHAGHEETEG TLGVAPRSTL LVQTPADVAA LNLPEGTQLS 190 200 210 220 230 240 YLTQTTLALD ETADVIDALR ARFPTLGQPP SEDICYATTN RQRALQSMVG ECDVVLVIGS 250 260 270 280 290 300 CNSSNSRRLV ELAQRSGTPA YLIDGPDDIE PEWLSSVSTI GVTAGASAPP RLVGQVIDAL 310 320 RGYASITVVE RSIATETVRF GLPKQVRAQ

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	BX842582 Genomic DNA. Translation: CAE55592.1. AE000516 Genomic DNA. Translation: AAK47825.1.
PIR	E70973.
RefSeq	NP_338011.1. NC_002755.2. YP_177967.1. NC_000962.2.
3D structure databases
ProteinModelPortal	P0A5I2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000001321; EBMYCP00000001321; EBMYCG00000001321. EBMYCT00000069759; EBMYCP00000067818; EBMYCG00000069754.
GeneID	887953. 926550.
GenomeReviews	Gene locus MT3490 in contig AE000516_GR. Gene locus Rv3382c in contig AL123456_GR.
KEGG	mtc:MT3490. mtu:Rv3382c.
PATRIC	18129419. VBIMycTub22151_3805.
TIGR	MT3490.
Organism-specific databases
TubercuList	Rv3382c.
Phylogenomic databases
GeneTree	EBGT00050000016858.
HOGENOM	HBG335228.
OMA	HNQGKRY.
PhylomeDB	P0A5I2.
ProtClustDB	CLSK799986.
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

ISPH2_MYCTU

Accession

Primary (citable) accession number: P0A5I2
Secondary accession number(s): O50409

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