UPPS_MICLU
ID UPPS_MICLU Reviewed; 249 AA.
AC O82827;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific);
DE EC=2.5.1.31;
DE AltName: Full=Ditrans,polycis-undecaprenylcistransferase;
DE AltName: Full=Undecaprenyl diphosphate synthase;
DE Short=UDS;
DE AltName: Full=Undecaprenyl pyrophosphate synthase;
DE Short=UPP synthase;
GN Name=uppS;
OS Micrococcus luteus (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=1270;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION AS AN
RP UNDECAPRENYL DIPHOSPHATE SYNTHASE, AND CATALYTIC ACTIVITY.
RC STRAIN=B-P 26;
RX PubMed=9677368; DOI=10.1074/jbc.273.31.19476;
RA Shimizu N., Koyama T., Ogura K.;
RT "Molecular cloning, expression, and purification of undecaprenyl
RT diphosphate synthase. No sequence similarity between E- and Z-prenyl
RT diphosphate synthases.";
RL J. Biol. Chem. 273:19476-19481(1998).
RN [2]
RP FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE SYNTHASE.
RC STRAIN=B-P 26;
RX PubMed=3182755; DOI=10.1093/oxfordjournals.jbchem.a122363;
RA Koyama T., Yoshida I., Ogura K.;
RT "Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26:
RT essential factors for the enzymatic activity.";
RL J. Biochem. 103:867-871(1988).
RN [3]
RP MUTAGENESIS OF ASN-77 AND TRP-78.
RC STRAIN=B-P 26;
RX PubMed=11098133; DOI=10.1093/oxfordjournals.jbchem.a022842;
RA Fujikura K., Zhang Y.W., Yoshizaki H., Nishino T., Koyama T.;
RT "Significance of Asn-77 and Trp-78 in the catalytic function of
RT undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26.";
RL J. Biochem. 128:917-922(2000).
RN [4]
RP MUTAGENESIS OF PHE-73; SER-74; GLU-193; ARG-197; GLU-201; ARG-203; GLU-216;
RP ASP-221 AND ASP-226.
RC STRAIN=B-P 26;
RX PubMed=11346651; DOI=10.1074/jbc.m102057200;
RA Kharel Y., Zhang Y.W., Fujihashi M., Miki K., Koyama T.;
RT "Identification of Significant residues for homoallylic substrate binding
RT of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase.";
RL J. Biol. Chem. 276:28459-28464(2001).
RN [5]
RP MUTAGENESIS OF ASP-29; GLY-32; ARG-33; ARG-42; GLU-76; ARG-80 AND GLU-84.
RC STRAIN=B-P 26;
RX PubMed=12680756; DOI=10.1021/bi027236v;
RA Fujikura K., Zhang Y.-W., Fujihashi M., Miki K., Koyama T.;
RT "Mutational analysis of allylic substrate binding site of Micrococcus
RT luteus B-P 26 undecaprenyl diphosphate synthase.";
RL Biochemistry 42:4035-4041(2003).
RN [6]
RP CRYSTALLIZATION.
RC STRAIN=B-P 26;
RX PubMed=10489461; DOI=10.1107/s0907444999008768;
RA Fujihashi M., Shimizu N., Zhang Y.W., Koyama T., Miki K.;
RT "Crystallization and preliminary X-ray diffraction studies of undecaprenyl
RT diphosphate synthase from Micrococcus luteus B-P 26.";
RL Acta Crystallogr. D 55:1606-1607(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RC STRAIN=B-P 26;
RX PubMed=11287651; DOI=10.1073/pnas.071514398;
RA Fujihashi M., Zhang Y.-W., Higuchi Y., Li X.-Y., Koyama T., Miki K.;
RT "Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl
RT diphosphate synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4337-4342(2001).
CC -!- FUNCTION: Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP)
CC from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate. UPP is
CC the precursor of glycosyl carrier lipid in the biosynthesis of
CC bacterial cell wall polysaccharide components such as peptidoglycan and
CC lipopolysaccharide. {ECO:0000269|PubMed:3182755,
CC ECO:0000269|PubMed:9677368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-
CC trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate;
CC Xref=Rhea:RHEA:27551, ChEBI:CHEBI:33019, ChEBI:CHEBI:58405,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.31;
CC Evidence={ECO:0000269|PubMed:9677368};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11287651}.
CC -!- DOMAIN: This enzyme shows a novel protein fold completely different
CC from the 'isoprenoid synthase fold' that is thought to be a common
CC structure for the enzymes relating to isoprenoid biosynthesis.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AB004319; BAA31993.1; -; Genomic_DNA.
DR PIR; T48857; T48857.
DR PDB; 1F75; X-ray; 2.20 A; A/B=1-249.
DR PDBsum; 1F75; -.
DR AlphaFoldDB; O82827; -.
DR SMR; O82827; -.
DR KEGG; ag:BAA31993; -.
DR BRENDA; 2.5.1.31; 3348.
DR EvolutionaryTrace; O82827; -.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..249
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123637"
FT ACT_SITE 29
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 30..33
FT /ligand="substrate"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="substrate"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74..76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 29
FT /note="D->A: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 32
FT /note="G->R: Great decrease in activity. Decrease in
FT activity; when associated with G-42."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 33
FT /note="R->A: Decrease in affinity for decaprenyl
FT diphosphate substrate analog."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 42
FT /note="R->G: Great decrease in activity. Decrease in
FT activity; when associated with R-32."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 73
FT /note="F->A: Decrease in activity; reduced affinity for
FT substrate."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 74
FT /note="S->A: Decrease in activity; reduced affinity for
FT substrate."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 76
FT /note="E->Q: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 77
FT /note="N->A,D,Q: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:11098133"
FT MUTAGEN 78
FT /note="W->I,R,D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11098133"
FT MUTAGEN 80
FT /note="R->A: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 84
FT /note="E->Q: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:12680756"
FT MUTAGEN 193
FT /note="E->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 197
FT /note="R->S: Great decrease in activity; reduced affinity
FT for substrate."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 201
FT /note="E->Q: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 203
FT /note="R->S: Great decrease in activity; reduced affinity
FT for substrate."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 216
FT /note="E->Q: Great decrease in activity; reduced affinity
FT for substrate."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 221
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11346651"
FT MUTAGEN 226
FT /note="D->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:11346651"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 42..63
FT /evidence="ECO:0007829|PDB:1F75"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:1F75"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1F75"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:1F75"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1F75"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1F75"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1F75"
FT TURN 209..214
FT /evidence="ECO:0007829|PDB:1F75"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1F75"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:1F75"
SQ SEQUENCE 249 AA; 28876 MW; 044F7DD77745AEEE CRC64;
MFPIKKRKAI KNNNINAAQI PKHIAIIMDG NGRWAKQKKM PRIKGHYEGM QTVKKITRYA
SDLGVKYLTL YAFSTENWSR PKDEVNYLMK LPGDFLNTFL PELIEKNVKV ETIGFIDDLP
DHTKKAVLEA KEKTKHNTGL TLVFALNYGG RKEIISAVQL IAERYKSGEI SLDEISETHF
NEYLFTANMP DPELLIRTSG EERLSNFLIW QCSYSEFVFI DEFWPDFNEE SLAQCISIYQ
NRHRRFGGL
