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 AGCAGTAACAGCAACACAAGTTTTATTTGCTAGCCAAGTTGGTTGAATATCACTTTTATC ATTAATGCGATATGATTCAATACCAATTTGTTCACCCATTGCAACTAATTTTAAGGTGTT ACTGCTACGATCATCACCAACAACAAGTAAAAGGTCAATTGTTGTTGGATCTAAACTTAG GACAGCATTTTGTCGTTCTAATGTTGCATTGCATAAATCATTTTTAAAAATAATTTCATT TGGAACAAGAGTTTTAAGTTTTTCAACAATTGCTTCAATATCAATTTTAGAAAGCGTTGT TTGGTTTGTAATTAAAATCTTTTTGGTTGGATCAAGATTGGGTAAAATGCTAGCAACTTC CTGTTCTGTTGTCACAAGATTGATGGTTGGACTAAGTGCTAACATTGCATTTGTTTCGGG ATGAAAGTGCTTCCCAATAAAAATAATTTGATAATCCGGTTTTGCTAAATATTCCTTAAT TAAATTTTTCGTAACTGTTACTCATTCACATTCAGTATCAACAAGTGTAATATTTTTTTG AACTGCAACATCTTTAATCCGATCATCACTACCATGGGCACTTAAAATCACAACAGCATT ATCTGGCAAAGTTTGAATTAACTCAAGGCGATTAAGTTTAAAATCATTAACAGGAATAAC ACCTAAGTTAACGATTTCATCAATGACATGTTTATTATGGACAAGATAACCTAACATATA AATTTGTCGCCCGGCATATTTAATAGCAGCTTCTTTTGCTCATTTAATTGATTTAACAAC ACCAAGACAATAACCACGAGGTGTTACTTTTACAACTTTCAT >protein sequence FKLNRLELIQTLPDNAVVILSAHGSDDRIKDVAVQKNITLVDTECEWVTVTKNLIKEYLA KPDYQIIFIGKHFHPETNAMLALSPTINLVTTEQEVASILPNLDPTKKILITNQTTLSKI DIEAIVEKLKTLVPNEIIFKNDLCNATLERQNAVLSLDPTTIDLLLVVGDDRSSNTLKLV AMGEQIGIESYRINDKSDIQPTWLANKTCVAVTAGASTPSIIQLEVIRYLEQI |
© Fisunov Lab of Proteomics, 2016.