位置:首页 > 蛋白库 > ISPH_DESVH
ISPH_DESVH
ID   ISPH_DESVH              Reviewed;         290 AA.
AC   Q72G08;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=DVU_0055;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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   -!- INTERACTION:
CC       Q72G08; Q72EB4: DVU_0664; NbExp=2; IntAct=EBI-10072158, EBI-10067158;
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00191}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017285; AAS94539.1; -; Genomic_DNA.
DR   RefSeq; WP_010937366.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009280.1; NC_002937.3.
DR   AlphaFoldDB; Q72G08; -.
DR   SMR; Q72G08; -.
DR   IntAct; Q72G08; 2.
DR   STRING; 882.DVU_0055; -.
DR   PaxDb; Q72G08; -.
DR   PRIDE; Q72G08; -.
DR   EnsemblBacteria; AAS94539; AAS94539; DVU_0055.
DR   KEGG; dvu:DVU_0055; -.
DR   PATRIC; fig|882.5.peg.55; -.
DR   eggNOG; COG0761; Bacteria.
DR   HOGENOM; CLU_027486_0_1_7; -.
DR   OMA; HNKYVVD; -.
DR   PhylomeDB; Q72G08; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000002194; 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   PANTHER; PTHR30426; PTHR30426; 1.
DR   Pfam; PF02401; LYTB; 1.
DR   TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..290
FT                   /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT                   /id="PRO_0000128811"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ   SEQUENCE   290 AA;  31527 MW;  525BEE04219A75BD CRC64;
     MNVIRARTAG FCMGVSLALR KLDREVDRAE EKAAQGSPRC RIATFGPIIH NPQVLEAYAG
     MGVRCLRQVD EVEAGDHVVI RAHGVPQQQE KALRSRDAVV VDATCPKVKK AQLGIEEQCR
     AGRTLLLFGE AEHPEVRGLL SYAGEGALVF GSVDELEGLP LQPETEYFLA AQTTQDRVAF
     EVARAWLHER LGHEVPVLET ICDATRLRQQ EAIDIARKVD AMVVVGGFDS GNTRRLADVA
     AAQGVFTVHV ENESQLPVEQ LRGCGIIGLT AGASTPKSII DATQRFLESL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024