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CRTE_CERS4
ID   CRTE_CERS4              Reviewed;         288 AA.
AC   P54976; Q3J195; Q9RFC5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Geranylgeranyl diphosphate synthase;
DE            Short=GGPP synthase;
DE            EC=2.5.1.29;
DE   AltName: Full=Farnesyltranstransferase;
GN   Name=crtE; OrderedLocusNames=RHOS4_18710; ORFNames=RSP_0265;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7721699; DOI=10.1128/jb.177.8.2064-2073.1995;
RA   Lang H.P., Cogdell R.J., Takaichi S., Hunter C.N.;
RT   "Complete DNA sequence, specific Tn5 insertion map, and gene assignment of
RT   the carotenoid biosynthesis pathway of Rhodobacter sphaeroides.";
RL   J. Bacteriol. 177:2064-2073(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA   Choudhary M., Kaplan S.;
RT   "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT   sphaeroides 2.4.1.";
RL   Nucleic Acids Res. 28:862-867(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of farnesyl diphosphate (FPP) and
CC       isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate
CC       (GGPP) needed for biosynthesis of carotenoids and diterpenes.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC         (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC         Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC       biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA79439.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ010302; CAB38744.1; -; Genomic_DNA.
DR   EMBL; AF195122; AAF24294.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA79439.2; ALT_INIT; Genomic_DNA.
DR   PIR; S49625; S49625.
DR   PIR; T50750; T50750.
DR   RefSeq; WP_011338112.1; NZ_AKVW01000001.1.
DR   RefSeq; YP_353340.2; NC_007493.2.
DR   AlphaFoldDB; P54976; -.
DR   SMR; P54976; -.
DR   STRING; 272943.RSP_0265; -.
DR   EnsemblBacteria; ABA79439; ABA79439; RSP_0265.
DR   KEGG; rsp:RSP_0265; -.
DR   PATRIC; fig|272943.9.peg.2209; -.
DR   eggNOG; COG0142; Bacteria.
DR   PhylomeDB; P54976; -.
DR   UniPathway; UPA00389; UER00564.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Chlorophyll biosynthesis; Isoprene biosynthesis;
KW   Magnesium; Metal-binding; Photosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="Geranylgeranyl diphosphate synthase"
FT                   /id="PRO_0000123995"
FT   BINDING         43
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         73
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         91
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         170
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        53
FT                   /note="A -> R (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="D -> S (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="A -> V (in Ref. 2; AAF24294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="R -> G (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="Q -> R (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="N -> S (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="R -> G (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="G -> A (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="E -> D (in Ref. 1; CAB38744)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  30229 MW;  FAB8D98C8557A8A2 CRC64;
     MAFEQRIEAA MAAAIARGQG SEAPSKLATA LDYAVTPGGA RIRPTLLLSV ATACGDDRPA
     LSDAAAVALE LIHCASLVHD DLPCFDDAEI RRGKPTVHRA YSEPLAILTG DSLIVMGFEV
     LARAAADQPQ RALQLVTALA VRTGMPMGIC AGQGWESESQ INLSAYHRAK TGALFIAATQ
     MGAIAAGYEA EPWEELGARI GEAFQVADDL RDALCDAETL GKPAGQDEIH ARPNAVREYG
     VEGAAKRLKD ILGGAIASIP SCPGEAMLAE MVRRYAEKIV PAQVAARV
 
 
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