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ISPH_MICAN
ID   ISPH_MICAN              Reviewed;         402 AA.
AC   B0JVA7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191};
DE            Short=HMBPP reductase {ECO:0000255|HAMAP-Rule:MF_00191};
DE            EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191};
GN   Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; OrderedLocusNames=MAE_16190;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
CC   -!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl
CC       4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP)
CC       and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the
CC       DOXP/MEP pathway for isoprenoid precursor biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC         + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:128753, ChEBI:CHEBI:128769; EC=1.17.7.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC         + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57623, ChEBI:CHEBI:128753; EC=1.17.7.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00191};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00191};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
CC       methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 6/6. {ECO:0000255|HAMAP-Rule:MF_00191}.
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00191}.
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DR   EMBL; AP009552; BAG01441.1; -; Genomic_DNA.
DR   RefSeq; WP_012264968.1; NC_010296.1.
DR   AlphaFoldDB; B0JVA7; -.
DR   SMR; B0JVA7; -.
DR   STRING; 449447.MAE_16190; -.
DR   PaxDb; B0JVA7; -.
DR   EnsemblBacteria; BAG01441; BAG01441; MAE_16190.
DR   KEGG; mar:MAE_16190; -.
DR   PATRIC; fig|449447.4.peg.1488; -.
DR   eggNOG; COG0761; Bacteria.
DR   HOGENOM; CLU_027486_4_0_3; -.
DR   OMA; HNKYVVD; -.
DR   OrthoDB; 1235756at2; -.
DR   BioCyc; MAER449447:MAE_RS07125-MON; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000001510; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13944; lytB_ispH; 1.
DR   HAMAP; MF_00191; IspH; 1.
DR   InterPro; IPR003451; LytB/IspH.
DR   Pfam; PF02401; LYTB; 1.
DR   TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..402
FT                   /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT                   /id="PRO_1000077519"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         157
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         288
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         317..319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   402 AA;  45595 MW;  CA57697354F754CB CRC64;
     MDTKSFKRTL QQSDNYNRKG FGHKEEVMDA MTNEYQSDLI QEIRENNYRL QRGDVTIYLA
     QAFGFCWGVE RAVAMAYETR QHFPQERIWI TNEIIHNPSV NQRLRSMAVG FIPVENGQKD
     FTVVESGDVV ILPAFGASVS EMQILNDKGC MIVDTTCPWV SKVWNSVEKH KKSDHTSIIH
     GKYNHEETIA TSSFAGTYLI VLNLDQANYV ANYILHGGDK NEFLEKFKNA HSQGFDPDRD
     LDYIGIANQT TMLKSETEEI GKLFEHTMLR KYGPIDFKDH FMSFNTICDA TQERQDAIFE
     LVKEPLSLMV VIGGYNSSNT THLQEIAIER AIPSYHIDSA ERILPGNRIE HKPLGDDLII
     TDNWLNEGKI VVGVTSGAST PDKVVEEVIE KIFAFKSSLV PG
 
 
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