ASD_METMA
ID ASD_METMA Reviewed; 208 AA.
AC Q8PX20;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Putative archaetidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664};
DE EC=4.1.1.- {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_00664}; OrderedLocusNames=MM_1402;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: Catalyzes the formation of archaetidylethanolamine (PtdEtn)
CC from archaetidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=archaetidylserine + H(+) = archaetidylethanolamine + CO2;
CC Xref=Rhea:RHEA:51488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:71517, ChEBI:CHEBI:134176; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00664};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00664};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00664};
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00664};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
CC {ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}.
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DR EMBL; AE008384; AAM31098.1; -; Genomic_DNA.
DR RefSeq; WP_011033348.1; NC_003901.1.
DR AlphaFoldDB; Q8PX20; -.
DR STRING; 192952.MM_1402; -.
DR EnsemblBacteria; AAM31098; AAM31098; MM_1402.
DR GeneID; 24879603; -.
DR GeneID; 66137164; -.
DR KEGG; mma:MM_1402; -.
DR PATRIC; fig|192952.21.peg.1624; -.
DR eggNOG; arCOG04470; Archaea.
DR HOGENOM; CLU_072492_1_0_2; -.
DR OMA; VSIFMSP; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00664; PS_decarb_PSD_A; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033175; PSD-A.
DR PANTHER; PTHR35809; PTHR35809; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00164; PS_decarb_rel; 1.
PE 3: Inferred from homology;
KW Cell membrane; Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Zymogen.
FT CHAIN 1..171
FT /note="Archaetidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029829"
FT CHAIN 172..208
FT /note="Archaetidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029830"
FT ACT_SITE 172
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 171..172
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 172
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 208 AA; 23416 MW; A69FF52D9751B42F CRC64;
MIAKGSEPWL FTAASVTALF AILSRATDGL PFLNYIANVG MALTFVMVIF FRDPERKVET
SDTYMISPAD GTVIDIRDRK ICIFMFLQNV HVNRAPISGK ISEIIYKKGG YLPAFCKDSE
RNERNEFIIH SKYGDVRVTQ IAGIIARRIV TYSNVNDTVE QGQRIGMIRF GSRVDVTIPH
DFDITVEKGE RVLAGKTIIA TIKNDRDF
