(data stored in ACNUC7421 zone)

SWISSPROT: PSD_PSEHT

ID   PSD_PSEHT               Reviewed;         288 AA.
AC   Q3IFN3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   05-JUL-2017, entry version 66.
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=PSHAa0486;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
CC       (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-
CC       Rule:MF_00662}.
CC   -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine =
CC       phosphatidylethanolamine + CO(2). {ECO:0000255|HAMAP-
CC       Rule:MF_00662}.
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00662};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00662};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2. {ECO:0000255|HAMAP-Rule:MF_00662}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
CC       and a small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00662}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00662}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00662}.
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:0000255|HAMAP-Rule:MF_00662}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00662}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI85582.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR954246; CAI85582.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011327195.1; NC_007481.1.
DR   STRING; 326442.PSHAa0486; -.
DR   EnsemblBacteria; CAI85582; CAI85582; PSHAa0486.
DR   GeneID; 32568091; -.
DR   KEGG; pha:PSHAa0486; -.
DR   eggNOG; ENOG4105DJ4; Bacteria.
DR   eggNOG; COG0688; LUCA.
DR   HOGENOM; HOG000282407; -.
DR   KO; K01613; -.
DR   OrthoDB; POG091H03XO; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-EC.
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; Q3IFN3.
DR   SWISS-2DPAGE; Q3IFN3.
KW   Cell membrane; Complete proteome; Decarboxylase; Lipid biosynthesis;
KW   Lipid metabolism; Lyase; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Pyruvate; Reference proteome; Zymogen.
FT   CHAIN         1    253       Phosphatidylserine decarboxylase beta
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00662}.
FT                                /FTId=PRO_0000262135.
FT   CHAIN       254    288       Phosphatidylserine decarboxylase alpha
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00662}.
FT                                /FTId=PRO_0000262136.
FT   ACT_SITE     91     91       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    148    148       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    254    254       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00662}.
FT   ACT_SITE    254    254       Schiff-base intermediate with substrate;
FT                                via pyruvic acid; for decarboxylase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00662}.
FT   SITE        253    254       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000255|HAMAP-
FT                                Rule:MF_00662}.
FT   MOD_RES     254    254       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00662}.
SQ   SEQUENCE   288 AA;  31432 MW;  A6DBA184438B262D CRC64;
     MSLDKFKIAM QYAMPKHFIS RVVGKLAAAK AGVLTTTLIK LFIKQYKVDM SEAKHPDPAH
     YESFNEFFTR PLKDGARPIV ADSDIIIHPV DGAISQLGDI VDGQLIQAKG HDYSLQALLG
     GNKDDTTPFL GGKFATIYLA PKDYHRIHMP IDGTLSKMIY VPGDLFSVNP LTAQNVPNLF
     ARNERVVAIF ETEIGPLAMV LVGATIVASI ETIWAGTVTP PAGSDVFSWN YPTKGENAIS
     LKKGEEMGRF KLGSTVVLAW GDDKADILDD QLPETVTRLG TPFAKIDD
//

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