PSD_ECOLI
ID PSD_ECOLI Reviewed; 322 AA.
AC P0A8K1; P10740; Q2M6E2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00662};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00662};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00662};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00662};
GN Name=psd {ECO:0000255|HAMAP-Rule:MF_00662};
GN OrderedLocusNames=b4160, JW4121;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE SITE,
RP FORMYLATION AT MET-1, PYRUVATE FORMATION AT SER-254, COFACTOR, AND SUBUNIT.
RX PubMed=3042771; DOI=10.1016/s0021-9258(18)37988-2;
RA Li Q.-X., Dowhan W.;
RT "Structural characterization of Escherichia coli phosphatidylserine
RT decarboxylase.";
RL J. Biol. Chem. 263:11516-11522(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=4598120; DOI=10.1016/s0021-9258(19)42640-9;
RA Dowhan W., Wickner W.T., Kennedy E.P.;
RT "Purification and properties of phosphatidylserine decarboxylase from
RT Escherichia coli.";
RL J. Biol. Chem. 249:3079-3084(1974).
RN [6]
RP ACTIVE SITE.
RX PubMed=338609; DOI=10.1016/s0021-9258(17)38234-0;
RA Satre M., Kennedy E.P.;
RT "Identification of bound pyruvate essential for the activity of
RT phosphatidylserine decarboxylase of Escherichia coli.";
RL J. Biol. Chem. 253:479-483(1978).
RN [7]
RP MUTAGENESIS OF SER-254.
RX PubMed=2406271; DOI=10.1016/s0021-9258(19)39709-1;
RA Li Q.-X., Dowhan W.;
RT "Studies on the mechanism of formation of the pyruvate prosthetic group of
RT phosphatidylserine decarboxylase from Escherichia coli.";
RL J. Biol. Chem. 265:4111-4115(1990).
RN [8]
RP REVIEW.
RX PubMed=1495415; DOI=10.1016/0076-6879(92)09043-3;
RA Dowhan W., Li Q.-X.;
RT "Phosphatidylserine decarboxylase from Escherichia coli.";
RL Methods Enzymol. 209:348-359(1992).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked
CC form of the serine moiety, and not serine alone or derivatives like
CC phosphoserine or glycerophosphoserine. {ECO:0000255|HAMAP-
CC Rule:MF_00662, ECO:0000269|PubMed:4598120}.
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:0000255|HAMAP-
CC Rule:MF_00662, ECO:0000269|PubMed:4598120};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00662,
CC ECO:0000269|PubMed:3042771};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00662, ECO:0000269|PubMed:3042771};
CC -!- ACTIVITY REGULATION: Inhibited by ionic detergents such as Barlox-12,
CC an amine oxide, and sodium dodecyl sulfate.
CC {ECO:0000269|PubMed:4598120}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:4598120};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00662, ECO:0000269|PubMed:3042771}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00662,
CC ECO:0000269|PubMed:4598120}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}.
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 (PubMed:3042771,
CC PubMed:2406271). During this reaction, the Ser that is part of the
CC protease active site of the proenzyme becomes the pyruvoyl prosthetic
CC group, which constitutes an essential element of the active site of the
CC mature decarboxylase (By similarity). {ECO:0000250|UniProtKB:B3L2V1,
CC ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:2406271,
CC ECO:0000269|PubMed:3042771}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Prokaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00662}.
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DR EMBL; J03916; AAA83896.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97059.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77120.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78164.1; -; Genomic_DNA.
DR PIR; A29234; A29234.
DR RefSeq; NP_418584.1; NC_000913.3.
DR RefSeq; WP_000934920.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P0A8K1; -.
DR SMR; P0A8K1; -.
DR BioGRID; 4261081; 79.
DR IntAct; P0A8K1; 2.
DR STRING; 511145.b4160; -.
DR jPOST; P0A8K1; -.
DR PaxDb; P0A8K1; -.
DR PRIDE; P0A8K1; -.
DR EnsemblBacteria; AAC77120; AAC77120; b4160.
DR EnsemblBacteria; BAE78164; BAE78164; BAE78164.
DR GeneID; 66671928; -.
DR GeneID; 948673; -.
DR KEGG; ecj:JW4121; -.
DR KEGG; eco:b4160; -.
DR PATRIC; fig|1411691.4.peg.2538; -.
DR EchoBASE; EB0768; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_029061_4_1_6; -.
DR InParanoid; P0A8K1; -.
DR OMA; KDYHHYH; -.
DR PhylomeDB; P0A8K1; -.
DR BioCyc; EcoCyc:PSD-MON; -.
DR BioCyc; MetaCyc:PSD-MON; -.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:P0A8K1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016540; P:protein autoprocessing; IMP:EcoCyc.
DR GO; GO:0031638; P:zymogen activation; IMP:EcoCyc.
DR HAMAP; MF_00662; PS_decarb_PSD_B_type1; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033178; PSD_type1_pro.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Decarboxylase; Direct protein sequencing; Formylation;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Zymogen.
FT CHAIN 1..253
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00662"
FT /id="PRO_0000029647"
FT CHAIN 254..322
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00662"
FT /id="PRO_0000029648"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_00662"
FT ACT_SITE 147
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_00662"
FT ACT_SITE 254
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_00662"
FT ACT_SITE 254
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00662,
FT ECO:0000305|PubMed:338609"
FT SITE 253..254
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00662,
FT ECO:0000269|PubMed:3042771"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:3042771"
FT MOD_RES 254
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00662,
FT ECO:0000269|PubMed:3042771"
FT MUTAGEN 254
FT /note="S->A: No processing of the proenzyme, complete loss
FT of activity."
FT /evidence="ECO:0000269|PubMed:2406271"
FT MUTAGEN 254
FT /note="S->C: Reduced processing, 16% wild-type activity."
FT /evidence="ECO:0000269|PubMed:2406271"
FT MUTAGEN 254
FT /note="S->T: Reduced processing, 2% wild-type activity."
FT /evidence="ECO:0000269|PubMed:2406271"
SQ SEQUENCE 322 AA; 35934 MW; 45195A6689610599 CRC64;
MLNSFKLSLQ YILPKLWLTR LAGWGASKRA GWLTKLVIDL FVKYYKVDMK EAQKPDTASY
RTFNEFFVRP LRDEVRPIDT DPNVLVMPAD GVISQLGKIE EDKILQAKGH NYSLEALLAG
NYLMADLFRN GTFVTTYLSP RDYHRVHMPC NGILREMIYV PGDLFSVNHL TAQNVPNLFA
RNERVICLFD TEFGPMAQIL VGATIVGSIE TVWAGTITPP REGIIKRWTW PAGENDGSVA
LLKGQEMGRF KLGSTVINLF APGKVNLVEQ LESLSVTKIG QPLAVSTETF VTPDAEPAPL
PAEEIEAEHD ASPLVDDKKD QV
