ID C9R646_AGGAD Unreviewed; 314 AA.
AC C9R646;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase;
DE EC=1.17.1.2;
GN Name=ispH; OrderedLocusNames=D11S_1928;
OS Aggregatibacter actinomycetemcomitans serotype C (strain D11S-1)
OS (Actinobacillus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=668336;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D11S-1;
RX PubMed=19820097; DOI=10.1128/JB.01203-09;
RA Chen C., Kittichotirat W., Si Y., Bumgarner R.;
RT "Genome sequence of Aggregatibacter actinomycetemcomitans serotype c
RT strain D11S-1.";
RL J. Bacteriol. 191:7378-7379(2009).
CC -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate
CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate
CC (DMAPP) (By similarity).
CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + NAD(P)(+) + H(2)O
CC = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H.
CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + NAD(P)(+) + H(2)O =
CC (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H.
CC -!- COFACTOR: Binds 1 3Fe-4S cluster per subunit (By similarity).
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
CC methylbutenyl diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC deoxy-D-xylulose 5-phosphate: step 6/6.
CC -!- SIMILARITY: Belongs to the IspH family.
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DR EMBL; CP001733; ACX83282.1; -; Genomic_DNA.
DR RefSeq; YP_003256501.1; NC_013416.1.
DR STRING; 668336.D11S_1928; -.
DR EnsemblBacteria; ACX83282; ACX83282; D11S_1928.
DR GeneID; 8537647; -.
DR KEGG; aat:D11S_1928; -.
DR PATRIC; 31914577; VBIAggAct139153_1810.
DR eggNOG; COG0761; -.
DR HOGENOM; HOG000220192; -.
DR KO; K03527; -.
DR OMA; QDAMFSL; -.
DR BioCyc; AACT668336:GJBF-1925-MONOMER; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:HAMAP.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway; IEA:HAMAP.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00191; IspH; 1; -.
DR InterPro; IPR003451; LytB.
DR Pfam; PF02401; LYTB; 1.
DR TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE 3: Inferred from homology;
KW 3Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis;
KW Metal-binding; NADP; Oxidoreductase.
FT REGION 225 227 Substrate binding (By similarity).
FT METAL 12 12 Iron-sulfur (3Fe-4S) (By similarity).
FT METAL 96 96 Iron-sulfur (3Fe-4S) (By similarity).
FT METAL 197 197 Iron-sulfur (3Fe-4S) (By similarity).
FT BINDING 41 41 Substrate (By similarity).
FT BINDING 74 74 Substrate (By similarity).
FT BINDING 124 124 Substrate (By similarity).
FT BINDING 167 167 Substrate (By similarity).
FT BINDING 269 269 Substrate (By similarity).
SQ SEQUENCE 314 AA; 34351 MW; E736689AD723CFE8 CRC64;
MKIILANPRG FCAGVDRAIS IVELALKIHG APIYVRHEVV HNRFVVNGLR ERGAIFVEEL
SEVPDGAIVI FSAHGVSQAV RQEAKERNLK VFDATCPLVT KVHMQVARAS RKGTKAILIG
HKGHPEVEGT MGQYGNQEGG IYLIESVEDI ANLPVKQNDD LTFMTQTTLS LDDTAETISA
LKEKYPAIQG PHKNDICYAT TNRQEAVREL AKQSDLVVVV GSKNSSNSNR LAELASRMGV
ASKLIDDPND IHANWFDGVQ TIGVTAGASA PEELVQSVIS RLKEFGVTTV EELQGLEENM
FFEVPKELRL KEAN
//
