(data stored in ACNUC7421 zone)

SWISSPROT: C3MHK1_SINFN

ID   C3MHK1_SINFN            Unreviewed;       336 AA.
AC   C3MHK1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772271};
DE            EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772271};
GN   Name=lytB {ECO:0000313|EMBL:ACP24329.1};
GN   Synonyms=ispH {ECO:0000256|HAMAP-Rule:MF_00191};
GN   OrderedLocusNames=NGR_c05330 {ECO:0000313|EMBL:ACP24329.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24329.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24329.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate
CC       into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate
CC       (DMAPP). {ECO:0000256|HAMAP-Rule:MF_00191,
CC       ECO:0000256|SAAS:SAAS00772275}.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized
CC       ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
CC       methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
CC       sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191,
CC       ECO:0000256|SAAS:SAAS00772240}.
CC   -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized
CC       ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
CC       methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
CC       sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191,
CC       ECO:0000256|SAAS:SAAS00772227}.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00191};
CC       Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS00772254}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS00772267}.
CC   -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00191, ECO:0000256|SAAS:SAAS00772194}.
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DR   EMBL; CP001389; ACP24329.1; -; Genomic_DNA.
DR   RefSeq; WP_012707114.1; NC_012587.1.
DR   RefSeq; YP_002825082.1; NC_012587.1.
DR   STRING; 394.NGR_c05330; -.
DR   EnsemblBacteria; ACP24329; ACP24329; NGR_c05330.
DR   GeneID; 7791759; -.
DR   KEGG; rhi:NGR_c05330; -.
DR   PATRIC; fig|394.7.peg.3346; -.
DR   eggNOG; ENOG4105C48; Bacteria.
DR   eggNOG; COG0761; LUCA.
DR   HOGENOM; HOG000220192; -.
DR   KO; K03527; -.
DR   OMA; TKVHKEA; -.
DR   OrthoDB; POG091H038O; -.
DR   UniPathway; UPA00056; UER00097.
DR   UniPathway; UPA00059; UER00105.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-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, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd13944; lytB_ispH; 1.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   HAMAP; MF_00191; IspH; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003451; LytB/IspH.
DR   PANTHER; PTHR30426; PTHR30426; 1.
DR   Pfam; PF02401; LYTB; 1.
DR   TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHK1.
DR   SWISS-2DPAGE; C3MHK1.
KW   3Fe-4S {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772246};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772206};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772258};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772198};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772260};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772202};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191,
KW   ECO:0000256|SAAS:SAAS00772211, ECO:0000313|EMBL:ACP24329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   REGION      236    238       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL        22     22       Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       109    109       Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   METAL       208    208       Iron-sulfur (3Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00191}.
FT   BINDING      51     51       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING      87     87       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     178    178       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
FT   BINDING     281    281       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00191}.
SQ   SEQUENCE   336 AA;  36411 MW;  7333939D5719FDF0 CRC64;
     MASSTAEKSP ITIRLCGPRG FCAGVDRAIQ IVVLALKEFG APVYVRHEIV HNRYVVEGLE
     AKGAIFVEEL DEIPPEHRKQ PVVFSAHGVP KSVPADADQR NLFYLDATCP LVSKVHKQAM
     RHHRLGRHVV LIGHAGHPEV IGTMGQLPEG TVSLIETVED ADAYVPPDPD NLGFVTQTTL
     SVDDTAGVIK RLHERFPNLT APAADSICYA TTNRQEAVKQ AAPGCDLFLV VGAPNSSNSK
     RLVEVALRAG AKHAVLVQRA SEIDWDTLGD ITTVGLSAGA SAPEVIVNEI IEAFRERYQA
     AVELADTVEE NENFLVNREL RHVELTAADM AFVNGE
//

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