AIPS_METTH
ID AIPS_METTH Reviewed; 195 AA.
AC O27726;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Archaetidylinositol phosphate synthase {ECO:0000303|PubMed:19740749};
DE Short=AIP synthase {ECO:0000303|PubMed:19740749};
DE EC=2.7.8.39 {ECO:0000269|PubMed:19740749};
GN OrderedLocusNames=MTH_1691;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=19740749; DOI=10.1074/jbc.m109.034652;
RA Morii H., Kiyonari S., Ishino Y., Koga Y.;
RT "A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-
RT myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in
RT methanoarchaeon Methanothermobacter thermautotrophicus cells.";
RL J. Biol. Chem. 284:30766-30774(2009).
CC -!- FUNCTION: Catalyzes the formation of archaetidylinositol phosphate
CC (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-
CC glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-
CC phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an
CC ether-type inositol phospholipid ubiquitously distributed in archaea
CC membranes and essential for glycolipid biosynthesis in archaea.
CC {ECO:0000269|PubMed:19740749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-
CC glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-
CC phosphate; Xref=Rhea:RHEA:36823, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58401, ChEBI:CHEBI:60377, ChEBI:CHEBI:74004,
CC ChEBI:CHEBI:74006; EC=2.7.8.39;
CC Evidence={ECO:0000269|PubMed:19740749};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19740749};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19740749};
CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000305|PubMed:19740749}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19740749};
CC Multi-pass membrane protein {ECO:0000305|PubMed:19740749}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000255|HAMAP-Rule:MF_02242, ECO:0000305}.
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DR EMBL; AE000666; AAB86163.1; -; Genomic_DNA.
DR PIR; B69093; B69093.
DR AlphaFoldDB; O27726; -.
DR SMR; O27726; -.
DR STRING; 187420.MTH_1691; -.
DR EnsemblBacteria; AAB86163; AAB86163; MTH_1691.
DR KEGG; mth:MTH_1691; -.
DR PATRIC; fig|187420.15.peg.1651; -.
DR HOGENOM; CLU_080384_1_2_2; -.
DR OMA; DGNMARQ; -.
DR BioCyc; MetaCyc:MON-15156; -.
DR BRENDA; 2.7.8.39; 3256.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1760; -; 1.
DR HAMAP; MF_02242; AIP_synthase; 1.
DR InterPro; IPR044270; AIP_synthase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW Membrane; Metal-binding; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..195
FT /note="Archaetidylinositol phosphate synthase"
FT /id="PRO_0000424146"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
SQ SEQUENCE 195 AA; 20895 MW; D1C0FBBFFFA41A25 CRC64;
MPDINESMLN QFRPVIRRFI DPIADRIALP ADYITLTGFL VACAASAGYA SGSLITGAAL
LAASGFIDVL DGAVARRRFR PTAFGGFLDS TLDRLSDGII IIGITAGGFT GLLTGLLALH
SGLMVSYVRA RAESLGIECA VGIAERAERI IIILAGSLAG YLIHPWFMDA AIIVLAALGY
FTMIQRMIYV WQRLK
