SPM_005665


  Uniprot: A0A037UNM6
Description: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
EC number: 1.17.7.4
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00605456}.; CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00605455}.
Cofactor: COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000256|HAMAP-Rule:MF_00191}; ; Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-Rule:MF_00191}
Enzyme regulation: 
Function [CC]: FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00096481}.
Pathway: PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00389088}.; PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00389010}.
Active site: 
Binding site: BINDING 42 42 Substrate. {ECO:0000256|HAMAP-Rule:MF_00191}.; BINDING 83 83 Substrate. {ECO:0000256|HAMAP-Rule:MF_00191}.; BINDING 134 134 Substrate. {ECO:0000256|HAMAP-Rule:MF_00191}.; BINDING 175 175 Substrate. {ECO:0000256|HAMAP-Rule:MF_00191}.; BINDING 277 277 Substrate. {ECO:0000256|HAMAP-Rule:MF_00191}.
Calcium binding: 
DNA binding: 
Metal binding: METAL 12 12 Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-Rule:MF_00191}.; METAL 105 105 Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-Rule:MF_00191}.; METAL 204 204 Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-Rule:MF_00191}.
Nucleotide binding: 
Site: 
Gene names (primary): ispH
Gene names (synonym): 
Mass: 32,638
Subunit structure [CC]: 
Gene ontology (GO): 3 iron, 4 sulfur cluster binding [GO:0051538]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity [GO:0051745]; metal ion binding [GO:0046872]; dimethylallyl diphosphate biosynthetic process [GO:0050992]; isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0019288]; terpenoid biosynthetic process [GO:0016114]
Gene ontology IDs: GO:0016114; GO:0019288; GO:0046872; GO:0050992; GO:0051538; GO:0051745
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00574269}.
Protein families: IspH family
Coiled coil: 
Domain [FT]: 
Motif: 
Region: REGION 233 235 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00191}.
EMBL: AGBZ02000004
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92218
UniPathway: 
CDD: 
Gene3D: cd13944
HAMAP: 
InterPro: MF_00191
PANTHER: IPR003451
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: 
ProDom: PF02401
SMART: 
SUPFAM: 
TIGRFAMs: 
197094-197976(-)

>nucleotide sequence
TTATATTTGTTCTAAATAACGAATTACTTCTAATTGGATGATACTAGGTGTTGATGCTCC
AGCAGTAACAGCAACACAAGTTTTATTTGCTAGCCAAGTTGGTTGAATATCACTTTTATC
ATTAATGCGATATGATTCAATACCAATTTGTTCACCCATTGCAACTAATTTTAAGGTGTT
ACTGCTACGATCATCACCAACAACAAGTAAAAGGTCAATTGTTGTTGGATCTAAACTTAG
GACAGCATTTTGTCGTTCTAATGTTGCATTGCATAAATCATTTTTAAAAATAATTTCATT
TGGAACAAGAGTTTTAAGTTTTTCAACAATTGCTTCAATATCAATTTTAGAAAGCGTTGT
TTGGTTTGTAATTAAAATCTTTTTGGTTGGATCAAGATTGGGTAAAATGCTAGCAACTTC
CTGTTCTGTTGTCACAAGATTGATGGTTGGACTAAGTGCTAACATTGCATTTGTTTCGGG
ATGAAAGTGCTTCCCAATAAAAATAATTTGATAATCCGGTTTTGCTAAATATTCCTTAAT
TAAATTTTTCGTAACTGTTACTCATTCACATTCAGTATCAACAAGTGTAATATTTTTTTG
AACTGCAACATCTTTAATCCGATCATCACTACCATGGGCACTTAAAATCACAACAGCATT
ATCTGGCAAAGTTTGAATTAACTCAAGGCGATTAAGTTTAAAATCATTAACAGGAATAAC
ACCTAAGTTAACGATTTCATCAATGACATGTTTATTATGGACAAGATAACCTAACATATA
AATTTGTCGCCCGGCATATTTAATAGCAGCTTCTTTTGCTCATTTAATTGATTTAACAAC
ACCAAGACAATAACCACGAGGTGTTACTTTTACAACTTTCAT


>protein sequence
MKVVKVTPRGYCLGVVKSIKWAKEAAIKYAGRQIYMLGYLVHNKHVIDEIVNLGVIPVND
FKLNRLELIQTLPDNAVVILSAHGSDDRIKDVAVQKNITLVDTECEWVTVTKNLIKEYLA
KPDYQIIFIGKHFHPETNAMLALSPTINLVTTEQEVASILPNLDPTKKILITNQTTLSKI
DIEAIVEKLKTLVPNEIIFKNDLCNATLERQNAVLSLDPTTIDLLLVVGDDRSSNTLKLV
AMGEQIGIESYRINDKSDIQPTWLANKTCVAVTAGASTPSIIQLEVIRYLEQI






















© Fisunov Lab of Proteomics, 2016.