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Database: UniProt
Entry: T0HU03_9SPHN
LinkDB: T0HU03_9SPHN
Original site: T0HU03_9SPHN 
ID   T0HU03_9SPHN            Unreviewed;       244 AA.
AC   T0HU03;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=RLDS_07260 {ECO:0000313|EMBL:EQB16607.1};
OS   Sphingobium lactosutens DS20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1331060 {ECO:0000313|EMBL:EQB16607.1, ECO:0000313|Proteomes:UP000015531};
RN   [1] {ECO:0000313|EMBL:EQB16607.1, ECO:0000313|Proteomes:UP000015531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS20 {ECO:0000313|EMBL:EQB16607.1,
RC   ECO:0000313|Proteomes:UP000015531};
RX   PubMed=24051323;
RA   Kumar R., Dwivedi V., Negi V., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium lactosutens Strain DS20T, Isolated
RT   from a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00753-13(2013).
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:EQB16607.1}.
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DR   EMBL; ATDP01000075; EQB16607.1; -; Genomic_DNA.
DR   RefSeq; WP_021225272.1; NZ_ATDP01000075.1.
DR   AlphaFoldDB; T0HU03; -.
DR   PATRIC; fig|1331060.3.peg.1368; -.
DR   eggNOG; COG0688; Bacteria.
DR   OrthoDB; 9790893at2; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000015531; 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..202
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023392008"
FT   CHAIN           203..244
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023392007"
FT   TRANSMEM        28..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        203
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   SITE            202..203
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   MOD_RES         203
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   244 AA;  26504 MW;  0C92ABC30B024B38 CRC64;
     MENNEITIAA GGNVKWRWPS VHPEGMKFGL IAAAITAVLF LVGWDIVGWL MLMVTIWVFA
     FFRDPVRAVP QDEGAIIAPA DGLVTLIQRV PPPREMAGVD GLGDQPLIRV SIFMSVFDVH
     INRTPIGGTI KSVVYISGKF LNADLDKASE DNERQHILVE RHDGLRIGFT QIAGLVARRI
     VPFVKPGDMV AAGQRIGLIR FGSRVDVYLP AGTAPRVILG QRTVAGETIL GQIGDARVVP
     GIQQ
//
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