ASD_METBF
ID ASD_METBF Reviewed; 203 AA.
AC Q46E43;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Mbar_A0875;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69849.1; -; Genomic_DNA.
DR RefSeq; WP_011305898.1; NC_007355.1.
DR AlphaFoldDB; Q46E43; -.
DR SMR; Q46E43; -.
DR STRING; 269797.Mbar_A0875; -.
DR EnsemblBacteria; AAZ69849; AAZ69849; Mbar_A0875.
DR GeneID; 3626183; -.
DR KEGG; mba:Mbar_A0875; -.
DR eggNOG; arCOG04470; Archaea.
DR HOGENOM; CLU_072492_1_0_2; -.
DR OMA; VSIFMSP; -.
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 Zymogen.
FT CHAIN 1..170
FT /note="Archaetidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000262285"
FT CHAIN 171..203
FT /note="Archaetidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000262286"
FT ACT_SITE 171
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 170..171
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 171
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 203 AA; 23036 MW; C8246C8E24C46189 CRC64;
MLAKGSEPWL FTATFITALF AVLSRAMNSS HLNHVAYIAM AMTFFMVLFF RDPERKVEVS
DTYMISPADG TVIDIRGRKI CIFMFLQNVH VNRAPISGKI REITYKKGGY LPAFCKDSER
NERNEFIIHS KYGDVSVMQI AGTIARRIVS YSRVNDNIEQ GQRIGMIRLG SRVDVTIPHD
FEIIVRKGER VLAGKTIIAT IKK
