SDSA_RHOCA
ID SDSA_RHOCA Reviewed; 325 AA.
AC O24743;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=All-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific);
DE EC=2.5.1.84;
DE AltName: Full=Solanesyl diphosphate synthase;
GN Name=sdsA; Synonyms=sds1;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A SOLANESYL DIPHOSPHATE
RP SYNTHASE, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC STRAIN=ATCC 23782 / LMG 2373 / NCIMB 11773 / St. Louis;
RX PubMed=9324242; DOI=10.1128/jb.179.19.5992-5998.1997;
RA Okada K., Kamiya Y., Zhu X., Suzuki K., Tanaka K., Nakagawa T., Matsuda H.,
RA Kawamukai M.;
RT "Cloning of the sdsA gene encoding solanesyl diphosphate synthase from
RT Rhodobacter capsulatus and its functional expression in Escherichia coli
RT and Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:5992-5998(1997).
CC -!- FUNCTION: catalyzes the sequential condensation of isopentenyl
CC diphosphate (IPP) with the allylic substrate to give solanesyl
CC diphosphate. Could be important to determine the side chain length of
CC ubiquinone. {ECO:0000269|PubMed:9324242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 7 isopentenyl diphosphate = all-
CC trans-nonaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:27563,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:58391,
CC ChEBI:CHEBI:128769; EC=2.5.1.84;
CC Evidence={ECO:0000269|PubMed:9324242};
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 -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB001997; BAA22867.1; -; Genomic_DNA.
DR AlphaFoldDB; O24743; -.
DR SMR; O24743; -.
DR BioCyc; MetaCyc:MON-13766; -.
DR GO; GO:0052923; F:all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; 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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..325
FT /note="All-trans-nonaprenyl-diphosphate synthase (geranyl-
FT diphosphate specific)"
FT /id="PRO_0000419190"
FT BINDING 48
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 51
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 81
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 174
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 35744 MW; DED1AA06304D9653 CRC64;
MAIDFKQDIL APVAQDFAAM DQFINEGISS KVALVMSVSK HVVEAGGKRM RPIMCLLAAY
ACGETNLKHA QKLAAIIEML HTATLVHDDV VDESGLRRGR PTANATWNNQ TAVLVGDFLI
ARAFDLLVDL DNMILLKDFS TGTCEIAEGE VLQLQAQHQP DTTEDIYLQI IHGKTSRLFE
LATEGAAILA GKPEYREPLR RFAGHFGNAF QIIDDILDYT SDADTLGKNI GDDLMEGKPT
LPLIAAMQNT QGEQRDLIRR SIATGGTSQL EQVIAIVQNS GALDYCHKRA TEETERALQA
LEILPESTYR QALVNLTRLA LDRIQ
