位置:首页 > 蛋白库 > PSD_RHORT
PSD_RHORT
ID   PSD_RHORT               Reviewed;         236 AA.
AC   Q2RNB6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664};
DE            EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664};
GN   Name=psd {ECO:0000255|HAMAP-Rule:MF_00664}; OrderedLocusNames=Rru_A3585;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00664}.
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_00664};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00664};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00664};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2. {ECO:0000255|HAMAP-Rule:MF_00664}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00664}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00664};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00664}.
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 post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
CC       {ECO:0000255|HAMAP-Rule:MF_00664}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}.
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; CP000230; ABC24379.1; -; Genomic_DNA.
DR   RefSeq; WP_011391332.1; NC_007643.1.
DR   RefSeq; YP_428666.1; NC_007643.1.
DR   AlphaFoldDB; Q2RNB6; -.
DR   STRING; 269796.Rru_A3585; -.
DR   EnsemblBacteria; ABC24379; ABC24379; Rru_A3585.
DR   KEGG; rru:Rru_A3585; -.
DR   PATRIC; fig|269796.9.peg.3706; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_072492_0_0_5; -.
DR   OMA; VSIFMSP; -.
DR   OrthoDB; 891720at2; -.
DR   PhylomeDB; Q2RNB6; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000001929; 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_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
DR   PANTHER; PTHR35809; PTHR35809; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00164; PS_decarb_rel; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW   Reference proteome; Zymogen.
FT   CHAIN           1..193
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_0000262263"
FT   CHAIN           194..236
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_0000262264"
FT   ACT_SITE        194
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT   SITE            193..194
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT   MOD_RES         194
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   236 AA;  25952 MW;  70F0660C71CCEA9E CRC64;
     MRRFDIGWKT YLLPEIHPEG WRFISIFAAV TFGLWLWQDW LVVPGLVLTI WCVYFFRNPK
     RTVPDRLGLV VTPASGIVQM VGLVDPPAEL ALDPPGPRQR ISVFMSVFDC HVNRCPVGGT
     VRKIVYAPGK FVNATLDKAS ADNERNSVVL DIGQSRDLAF VQIAGLVARR IRCDLVEGQS
     VLTGEIMGLI RFGSRLDIYL PPGAAPLVAP GQSCISGETV LADLASAEPE RLGVLR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024