ARSS_METTH
ID ARSS_METTH Reviewed; 233 AA.
AC O27106;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Archaetidylserine synthase;
DE EC=2.7.8.38;
DE AltName: Full=CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase;
GN OrderedLocusNames=MTH_1027;
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, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=12562787; DOI=10.1128/jb.185.4.1181-1189.2003;
RA Morii H., Koga Y.;
RT "CDP-2,3-Di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase
RT (archaetidylserine synthase) in the methanogenic archaeon
RT Methanothermobacter thermautotrophicus.";
RL J. Bacteriol. 185:1181-1189(2003).
CC -!- FUNCTION: Involved in the lipid biosynthesis. Catalyzes the formation
CC of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-
CC serine. Activity with ester-linked substrate analogs containing
CC straight aliphatic chains (typical bacterial substrates) is two to
CC three times higher than that with the corresponding ether-type
CC substrate (typical archaeal substrates). Both enantiomers of CDP-
CC unsaturated archaeols with ether-linked geranylgeranyl chains and CDP-
CC saturated archaeol with ether-linked phytanyl chains are similarly
CC active. The enzyme also accepts D-serine, although activity is only
CC about third of that with L-serine. {ECO:0000269|PubMed:12562787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + L-serine =
CC archaetidylserine + CMP + H(+); Xref=Rhea:RHEA:35439,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:58838,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:71517; EC=2.7.8.38;
CC Evidence={ECO:0000269|PubMed:12562787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-2,3-bis-O-(phytanyl)-sn-glycerol + L-serine = 2,3-bis-O-
CC phytanyl-sn-glycero-3-phospho-L-serine + CMP + H(+);
CC Xref=Rhea:RHEA:37367, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:74004, ChEBI:CHEBI:74853; EC=2.7.8.38;
CC Evidence={ECO:0000269|PubMed:12562787};
CC -!- ACTIVITY REGULATION: Activated by Mn(2+) ions.
CC {ECO:0000269|PubMed:12562787}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 8 and 8.5. {ECO:0000269|PubMed:12562787};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:12562787};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:12562787}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85523.1; -; Genomic_DNA.
DR PIR; A69004; A69004.
DR AlphaFoldDB; O27106; -.
DR SMR; O27106; -.
DR STRING; 187420.MTH_1027; -.
DR EnsemblBacteria; AAB85523; AAB85523; MTH_1027.
DR KEGG; mth:MTH_1027; -.
DR PATRIC; fig|187420.15.peg.1010; -.
DR HOGENOM; CLU_049944_3_1_2; -.
DR OMA; YSICGML; -.
DR BioCyc; MetaCyc:MON-14511; -.
DR BRENDA; 2.7.8.38; 3256.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043761; F:archaetidylserine synthase activity; IDA:UniProtKB.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR TIGRFAMs; TIGR00473; pssA; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..233
FT /note="Archaetidylserine synthase"
FT /id="PRO_0000422924"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 24618 MW; E91E7D7416E1BC63 CRC64;
MMNDKKITSF IALPDLLSML NASSGYLSIL LSIDGSLNAA CILMLLAVLF DSLDGWVARK
TGRIDIHGFG KNMDSLSDVI SFGVAPAILI YSAAVDFRYI NILVGPLIVL CGILRLSRFN
VLTGGGKNFT GLPIPVAAVT ISSFYLTGFY SELSAAFIMI AVSVLMISSI EYPRVDGMGA
STALILIIAT IISVAAVEIL QAASVVAGPV AIILFIATLT YIAVPILPKR DVI
