GenomeNet

Database: UniProt
Entry: M4U3T7_9GAMM
LinkDB: M4U3T7_9GAMM
Original site: M4U3T7_9GAMM 
ID   M4U3T7_9GAMM            Unreviewed;       300 AA.
AC   M4U3T7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00662};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00662};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00662};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00662};
GN   Name=psd {ECO:0000256|HAMAP-Rule:MF_00662};
GN   ORFNames=PCNPT3_01645 {ECO:0000313|EMBL:AGH80271.1};
OS   Psychromonas sp. CNPT3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80271.1, ECO:0000313|Proteomes:UP000010320};
RN   [1] {ECO:0000313|EMBL:AGH80271.1, ECO:0000313|Proteomes:UP000010320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80271.1,
RC   ECO:0000313|Proteomes:UP000010320};
RA   Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA   Yayanos A.A., Bartlett D.H.;
RT   "The complete genome sequence of the deep-sea bacterium Psychromonas
RT   CNPT2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00662}.
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_00662};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00662};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00662};
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_00662}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00662}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00662};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00662}.
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_00662}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-B subfamily. Prokaryotic type I sub-subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00662}.
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; CP004404; AGH80271.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4U3T7; -.
DR   STRING; 314282.PCNPT3_01645; -.
DR   KEGG; psy:PCNPT3_01645; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_029061_4_1_6; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000010320; 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:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00662; PS_decarb_PSD_B_type1; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033177; PSD-B.
DR   InterPro; IPR033178; PSD_type1_pro.
DR   NCBIfam; TIGR00163; PS_decarb; 1.
DR   PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00662};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00662}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00662};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00662};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010320};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00662}.
FT   CHAIN           1..264
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023249237"
FT   CHAIN           265..300
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023249236"
FT   ACT_SITE        108
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        165
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        265
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        265
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   SITE            264..265
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   MOD_RES         265
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
SQ   SEQUENCE   300 AA;  33152 MW;  D8957BFCE8B573E7 CRC64;
     MMQKMHVIVL PILIKENMMI DQLKIISQYL LPKHLLSRLT GKMAAAKAGK LTTFLITRFI
     SQYGIDMSEA KHSEAEDFDT FNDFFTRELK EGIRPIISGD ENLALPVDGK ISQQGDIKAG
     RIFQAKGHDF SLRELLGGQD AISAPFEDGI FSTIYLAPKD YHRIHMPITG KLEKTIFIPG
     DLFSVNPLTA ENVPNLFARN ERAVAIFSTA VGPMAMVLVG ATIVASIETV WSGTFKGKEI
     QYWDHSDEDI VLEKGAEMGR FKLGSTIVAL FAKDAIELSS ALEPGSVTRL GELFASTKQK
//
DBGET integrated database retrieval system