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Database: UniProt
Entry: A0A0A7V976_9ARCH
LinkDB: A0A0A7V976_9ARCH
Original site: A0A0A7V976_9ARCH 
ID   A0A0A7V976_9ARCH        Unreviewed;       246 AA.
AC   A0A0A7V976;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE            Short=GGGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE            Short=GGGPS {ECO:0000256|HAMAP-Rule:MF_00112};
DE            EC=2.5.1.41 {ECO:0000256|HAMAP-Rule:MF_00112};
DE   AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE   AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN   ORFNames=A7X95_05075 {ECO:0000313|EMBL:PTL87281.1}, T478_1498
GN   {ECO:0000313|EMBL:AJA93205.1};
OS   Candidatus Nitrosopelagicus brevis.
OC   Archaea; Nitrososphaerota.
OX   NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA93205.1, ECO:0000313|Proteomes:UP000030944};
RN   [1] {ECO:0000313|EMBL:AJA93205.1, ECO:0000313|Proteomes:UP000030944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN25 {ECO:0000313|EMBL:AJA93205.1}, and V2
RC   {ECO:0000313|Proteomes:UP000030944};
RX   PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA   Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA   McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT   "Genomic and proteomic characterization of "Candidatus Nitrosopelagicus
RT   brevis": an ammonia-oxidizing archaeon from the open ocean.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN   [2] {ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA   Dupont C., Santoro A.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PTL87281.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87281.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:PTL87281.1, ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87281.1,
RC   ECO:0000313|Proteomes:UP000241022};
RA   Carini P.;
RT   "Transcriptomics of ammonia oxidizing archaea.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC       geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3
CC       hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first
CC       ether-bond-formation step in the biosynthesis of archaeal membrane
CC       lipids. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-
CC         phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-
CC         phosphate; Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57677, ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00000742, ECO:0000256|HAMAP-
CC         Rule:MF_00112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00112}.
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DR   EMBL; CP007026; AJA93205.1; -; Genomic_DNA.
DR   EMBL; LXWN01000002; PTL87281.1; -; Genomic_DNA.
DR   RefSeq; WP_048106578.1; NZ_LXWN01000002.1.
DR   AlphaFoldDB; A0A0A7V976; -.
DR   STRING; 1410606.T478_1498; -.
DR   GeneID; 24817362; -.
DR   KEGG; nbv:T478_1498; -.
DR   HOGENOM; CLU_068610_0_0_2; -.
DR   OrthoDB; 7409at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000030944; Chromosome.
DR   Proteomes; UP000241022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase 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; FMN-linked oxidoreductases; 1.
DR   HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR   InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR   InterPro; IPR008205; GGGP_HepGP_synthase.
DR   InterPro; IPR010946; GGGP_synth.
DR   NCBIfam; TIGR01769; GGGP; 1.
DR   NCBIfam; TIGR01768; GGGP-family; 1.
DR   PANTHER; PTHR21235:SF22; GERANYLGERANYLGLYCERYL PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR   Pfam; PF01884; PcrB; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00112};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00112};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00112};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00112};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_00112};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_00112};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00112}.
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         172..178
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         203..204
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         225..226
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   246 AA;  26066 MW;  A6EEBA8F6A890C73 CRC64;
     MTGKVEELLL SERKKSPLLF VLIDSEVSQI DSAVKLAKDV EQIGAASILV GGSSATDQME
     MAEVVKNLKS AVNIPIILFP GNITGVVPQA DAILFSSLMN SENPYYITQA QALGAPNVLK
     FGLEPLPTSY LVIGEGTSAW FVGNVRGIPF DKPKIAAAYS LAAQFFGMRF VYLEAGSGAK
     TNVTPEMVAT VRKVFQGFLI VGGGIRDAQT AKSLTDAGAD ALVIGTLLED SKNLEKLTEI
     AKAIKN
//
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