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Database: UniProt
Entry: A0A1Y2T568_SYMTR
LinkDB: A0A1Y2T568_SYMTR
Original site: A0A1Y2T568_SYMTR 
ID   A0A1Y2T568_SYMTR        Unreviewed;       212 AA.
AC   A0A1Y2T568;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00664};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00664};
GN   Name=psd {ECO:0000256|HAMAP-Rule:MF_00664};
GN   ORFNames=A6D92_05265 {ECO:0000313|EMBL:OTA41600.1}, CWE10_00380
GN   {ECO:0000313|EMBL:MBY6274665.1};
OS   Symbiobacterium thermophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=2734 {ECO:0000313|EMBL:OTA41600.1, ECO:0000313|Proteomes:UP000194267};
RN   [1] {ECO:0000313|Proteomes:UP000194267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antunes L.P., Martins L.F., Pereira R.V., Thomas A.M., Barbosa D.,
RA   Nascimento L., Silva G.M., Condomitti G.W., Digiampietri L.A.,
RA   Lombardi K.C., Ramos P.L., Quaggio R.B., Oliveira J.C., Pascon R.C.,
RA   Cruz J.B., Silva A.M., Setubal J.C.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OTA41600.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2 {ECO:0000313|EMBL:OTA41600.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MBY6274665.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ZCTH01-B2 {ECO:0000313|EMBL:MBY6274665.1};
RA   Quaggio R., Amgarten D., Setubal J.C.;
RT   "Three new genomes from thermophilic consortium.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC         diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262,
CC         ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00664};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00664};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00664};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00664}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664};
CC       Peripheral membrane protein {ECO:0000256|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:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-A subfamily. {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OTA41600.1}.
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DR   EMBL; PIUK01000001; MBY6274665.1; -; Genomic_DNA.
DR   EMBL; LWLV01000339; OTA41600.1; -; Genomic_DNA.
DR   RefSeq; WP_043713825.1; NZ_PIUK01000001.1.
DR   AlphaFoldDB; A0A1Y2T568; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000194267; Unassembled WGS sequence.
DR   Proteomes; UP000732377; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
DR   PANTHER; PTHR35809; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR   PANTHER; PTHR35809:SF1; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00664}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00664, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00664}.
FT   CHAIN           1..179
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023562995"
FT   CHAIN           180..212
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023562996"
FT   TRANSMEM        12..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        180
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   SITE            179..180
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   MOD_RES         180
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   212 AA;  23410 MW;  96CFFBCC794846D0 CRC64;
     MRRPIIAREG WPFVGALVAL AVLALFVHWA LGAVLAGLAL FVMWFFRDPE RPIPREDGLV
     VSPADGRVMF VREVEEPRFV GGRALLVSIF LSVFDVHINR SPVAGEVTYR EYVPGKFLAA
     WDDTVGEVNE RAYLGLVTDG GHRVLVSQVA GLLARRIVTW PAVGDRLDRG QRFGLIRFGS
     CTQVWLPADS EVLVRPGDRV VAGQTVIGRL PQ
//
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