ID A0A0D9NYY6_METAN Unreviewed; 327 AA.
AC A0A0D9NYY6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyldiphosphate specific] {ECO:0000256|ARBA:ARBA00012596};
DE EC=2.5.1.87 {ECO:0000256|ARBA:ARBA00012596};
GN ORFNames=H634G_06762 {ECO:0000313|EMBL:KJK77795.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK77795.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87; Evidence={ECO:0000256|ARBA:ARBA00000976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the UPP synthase family.
CC {ECO:0000256|ARBA:ARBA00005432}.
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DR EMBL; KE384737; KJK77795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9NYY6; -.
DR STRING; 1291518.A0A0D9NYY6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IEA:InterPro.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019408; P:dolichol biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR InterPro; IPR038887; Nus1/NgBR.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR21528:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT NUS1; 1.
DR PANTHER; PTHR21528; UNCHARACTERIZED; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 327 AA; 37203 MW; 635457F093691923 CRC64;
MPMSARDRAA YRADDASDHK FLSAKERERI MRANLPNPNE IPTVAASKAQ SQRRSRLGVR
RFLKTQLYAL VFAIMHGLFS LYIRIRQAIH IVSYQVSSVL YYHHGTPEYI RRDIIGLGRK
PNHLSAILKA EENQRPKADL DRLIEETAEL AAWCASAEIP MLSIYEKTGI LKKHMPRVYE
AVMQKFTFYF AGQHPSLLLT SPHKDAYSSP ALAGDKHGHL KLHLISAQDG RESIVDLTRT
LAEMSQRGKI SPRDISMELV DAELSEGIMP EPDLLILFSP NVELSGYPPW QIRLTEIFCL
QDNEGFGYQV FLKALRKFAK AQMRNGK
//
