(data stored in ACNUC7421 zone)

SWISSPROT: PCRB_EXIS2

ID   PCRB_EXIS2              Reviewed;         227 AA.
AC   B1YJ15;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            Short=HepGP synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            EC=2.5.1.n9 {ECO:0000255|HAMAP-Rule:MF_00112};
DE   AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN   Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112}; OrderedLocusNames=Exig_0463;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the
CC       heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon
CC       atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing
CC       heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-
CC       formation step in the biosynthesis of archaea-type G1P-based membrane
CC       lipids found in Bacillales. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate =
CC         3-heptaprenyl-sn-glycero-1-phosphate + diphosphate;
CC         Xref=Rhea:RHEA:33495, ChEBI:CHEBI:33019, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:58206, ChEBI:CHEBI:64781; EC=2.5.1.n9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
DR   EMBL; CP001022; ACB59945.1; -; Genomic_DNA.
DR   RefSeq; WP_012369369.1; NC_010556.1.
DR   SMR; B1YJ15; -.
DR   STRING; 262543.Exig_0463; -.
DR   EnsemblBacteria; ACB59945; ACB59945; Exig_0463.
DR   KEGG; esi:Exig_0463; -.
DR   eggNOG; ENOG4108RTE; Bacteria.
DR   eggNOG; COG1646; LUCA.
DR   HOGENOM; HOG000015607; -.
DR   KO; K07094; -.
DR   OMA; TGAHKEW; -.
DR   OrthoDB; 1439634at2; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001681; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02812; PcrB_like; 1.
DR   Gene3D; 3.20.20.390; -; 1.
DR   HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR   InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR   InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR   InterPro; IPR008205; GGGP_HepGP_synthase.
DR   PANTHER; PTHR40029; PTHR40029; 1.
DR   Pfam; PF01884; PcrB; 1.
DR   TIGRFAMs; TIGR01768; GGGP-family; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1YJ15.
DR   SWISS-2DPAGE; B1YJ15.
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT   CHAIN           1..227
FT                   /note="Heptaprenylglyceryl phosphate synthase"
FT                   /id="PRO_0000350669"
FT   REGION          159..164
FT                   /note="Glycerol-1-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   REGION          209..210
FT                   /note="Glycerol-1-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   METAL           15
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   METAL           41
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         13
FT                   /note="Glycerol-1-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         189
FT                   /note="Glycerol-1-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   227 AA;  24751 MW;  2B5551670A785B09 CRC64;
     MLLPYNEWRH VFKLDPAKEI EEAALQAIAT SGTDAIIVGG TDDITLDATL DLLMRLRRYP
     VAVALEVSEL EAATMGFDAY LTPSVLNSGT LEHVIDKQVE ALEEVGHMLA HQDLVGEGYI
     VLNADAKVAR VTQAKLLNDD QVVAYAQLAD SVFRMPIIYL EYSGMYGDPS LVASVKRVLK
     QGRLFYGGGI DSIERAQEML THADTIVVGN IIYDNLEAAL ATVAATR
//

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