ID A0A1Y2PCF5_9FLAO Unreviewed; 292 AA.
AC A0A1Y2PCF5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00663};
DE EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00663};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00663};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00663};
GN Name=psd {ECO:0000256|HAMAP-Rule:MF_00663};
GN ORFNames=WH52_08900 {ECO:0000313|EMBL:OSY88125.1};
OS Tenacibaculum holothuriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1635173 {ECO:0000313|EMBL:OSY88125.1, ECO:0000313|Proteomes:UP000194221};
RN [1] {ECO:0000313|EMBL:OSY88125.1, ECO:0000313|Proteomes:UP000194221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-2 {ECO:0000313|EMBL:OSY88125.1,
RC ECO:0000313|Proteomes:UP000194221};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Tenacibaculum sp. S2-2, isolated from intestinal
RT microbiota of sea cucumber, Apostichopus japonicas.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00663}.
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_00663};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00663};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00663};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000256|HAMAP-Rule:MF_00663}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00663}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00663};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00663}.
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 autoendoproteolytic
CC cleavage occurs by a canonical serine protease mechanism, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to produce ammonia
CC and the pyruvoyl prosthetic group on the alpha chain. During this
CC reaction, the Ser that is part of the protease active site of the
CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000256|HAMAP-Rule:MF_00663}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Prokaryotic type II sub-subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00663}.
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:OSY88125.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAPZ01000005; OSY88125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2PCF5; -.
DR STRING; 1635173.WH52_08900; -.
DR InParanoid; A0A1Y2PCF5; -.
DR OrthoDB; 9802030at2; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000194221; 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_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD-B.
DR InterPro; IPR033179; PSD_type2_pro.
DR NCBIfam; TIGR00163; PS_decarb; 1.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00663};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00663};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00663};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00663};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00663};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00663};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00663};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00663};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00663};
KW Reference proteome {ECO:0000313|Proteomes:UP000194221};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00663}.
FT CHAIN 1..254
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT /id="PRO_5023574943"
FT CHAIN 255..292
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT /id="PRO_5023574942"
FT ACT_SITE 111
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT ACT_SITE 167
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT ACT_SITE 255
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT ACT_SITE 255
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT SITE 254..255
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
FT MOD_RES 255
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00663"
SQ SEQUENCE 292 AA; 33134 MW; 00D003CDFE90F372 CRC64;
MEIKFIDRKT GKTEIETPPG VGFLKFLYHN PFGKLAILPI AKRKFLSTWY GKKMDNPSST
KKIEVFVNQL NIDMSEAEKS ISEFTSFNDF FYRKLKPNAR PIQNGFVSPG DGKLLAFENI
SDVHNFFIKG RKFTLKEFLA SDTLAEKYKN ASLIILRLAP NDYHRYHFPY SGTPTEMTKI
KGDYYSVSPY ALASNFTKVF CENKREYCEL KTEDKGDILI APVGATMVGS IIETFTPNSS
IKKGDEMGYF AFGGSTIVLL VDKDKLKIDS DILQNTQNKT ETFVKMGEEI GM
//
