(data stored in SCRATCH zone)

SWISSPROT: C5BDM2_EDWI9

ID   C5BDM2_EDWI9            Unreviewed;       299 AA.
AC   C5BDM2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   30-AUG-2017, entry version 60.
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   OrderedLocusNames=NT01EI_0397 {ECO:0000313|EMBL:ACR67638.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67638.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
CC       (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-
CC       Rule:MF_00662, ECO:0000256|SAAS:SAAS00669590}.
CC   -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine =
CC       phosphatidylethanolamine + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00662, ECO:0000256|SAAS:SAAS00669619}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2. {ECO:0000256|HAMAP-Rule:MF_00662,
CC       ECO:0000256|SAAS:SAAS00669588}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
CC       and a small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00662, ECO:0000256|SAAS:SAAS00573303}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00662, ECO:0000256|SAAS:SAAS00669456}; Peripheral membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_00662,
CC       ECO:0000256|SAAS:SAAS00669456}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The autoendoproteolytic cleavage occurs by a
CC       canonical serine protease mechanism, in which the side chain
CC       hydroxyl group of the serine supplies its oxygen atom to form the
CC       C-terminus of the beta chain, while the remainder of the serine
CC       residue undergoes an oxidative deamination to produce ammonia and
CC       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
CC       an essential element of the active site of the mature
CC       decarboxylase. {ECO:0000256|HAMAP-Rule:MF_00662}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
CC       {ECO:0000256|SAAS:SAAS00669471}.
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DR   EMBL; CP001600; ACR67638.2; -; Genomic_DNA.
DR   STRING; 634503.NT01EI_0397; -.
DR   EnsemblBacteria; ACR67638; ACR67638; NT01EI_0397.
DR   KEGG; eic:NT01EI_0397; -.
DR   eggNOG; ENOG4105DJ4; Bacteria.
DR   eggNOG; COG0688; LUCA.
DR   HOGENOM; HOG000282407; -.
DR   KO; K01613; -.
DR   OrthoDB; POG091H03XO; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-HAMAP.
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.
DR   InterPro; IPR033178; PSD_type1_pro.
DR   PANTHER; PTHR10067; PTHR10067; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00163; PS_decarb; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BDM2.
DR   SWISS-2DPAGE; C5BDM2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00669466};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00093386};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00464072};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00093364};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00662, ECO:0000256|SAAS:SAAS00093332,
KW   ECO:0000313|EMBL:ACR67638.2};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00669459};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00093337};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00093406};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00662,
KW   ECO:0000256|SAAS:SAAS00093377};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00662}.
FT   ACT_SITE     90     90       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    147    147       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    253    253       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    253    253       Schiff-base intermediate with substrate;
FT                                via pyruvic acid; for decarboxylase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00662}.
FT   SITE        252    253       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_00662}.
FT   MOD_RES     253    253       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00662}.
SQ   SEQUENCE   299 AA;  32863 MW;  1346E7C353DEB14C CRC64;
     MLDSIKIRLQ YLLPKQGLTR LAGWAADKPA GWLTQSAIKG FARYYGINMQ EALYPDPAHY
     KTFNDFFVRP LRDGVRPLAE FDDGVVLPAD GAISQLGPID EDRILQAKGH DYTLEALLAG
     QYPLAETFRG GQFVTTYLSP RDYHRVHMPC DGQLREMIYV PGDLFSVNPL TAANVPNLFA
     RNERLICIFD TAFGPLAQIL VGATIVGSIE TVWDGCVNSE RAGIIRRWTY PAEGERAVAL
     KKGQEMGRFK LGSTVINLFA PGRIQFDCAL SAGCITRMGR ELGHAPAAAQ ESAANAEPT
//

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