PSD_RHIME
ID PSD_RHIME Reviewed; 232 AA.
AC Q9FDI9;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664, ECO:0000303|PubMed:18708506};
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, ECO:0000303|PubMed:18708506};
GN OrderedLocusNames=R01121; ORFNames=SMc00551;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA de Rudder K.E.E., Lopez-Lara I.M., Roehrs V., Geiger O.;
RT "Phosphatidylethanolamine is not essential for growth of Sinorhizobium
RT meliloti.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18708506; DOI=10.1128/jb.00610-08;
RA Vences-Guzman M.A., Geiger O., Sohlenkamp C.;
RT "Sinorhizobium meliloti mutants deficient in phosphatidylserine
RT decarboxylase accumulate phosphatidylserine and are strongly affected
RT during symbiosis with alfalfa.";
RL J. Bacteriol. 190:6846-6856(2008).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Important for establishment of root
CC nodule symbiosis with the host plant. {ECO:0000255|HAMAP-Rule:MF_00664,
CC ECO:0000269|PubMed:18708506}.
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;
CC Evidence={ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
CC Rule:MF_00664};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_00664};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-Rule:MF_00664};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000250|UniProtKB:P0A8K1, 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:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_00664}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0A8K1, 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:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- DISRUPTION PHENOTYPE: Initiates nodule formation in the alfalfa host
CC plant much later than the wild-type and forms 90% fewer nodules. The
CC nodules are almost devoid of bacteria and are unable to fix nitrogen.
CC {ECO:0000269|PubMed:18708506}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}.
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DR EMBL; AF247564; AAG00421.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45700.1; -; Genomic_DNA.
DR RefSeq; NP_385227.1; NC_003047.1.
DR RefSeq; WP_010969055.1; NC_003047.1.
DR AlphaFoldDB; Q9FDI9; -.
DR STRING; 266834.SMc00551; -.
DR EnsemblBacteria; CAC45700; CAC45700; SMc00551.
DR GeneID; 61602580; -.
DR KEGG; sme:SMc00551; -.
DR PATRIC; fig|266834.11.peg.2529; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_072492_0_0_5; -.
DR OMA; VSIFMSP; -.
DR BRENDA; 4.1.1.65; 10656.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000001976; 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..189
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029799"
FT CHAIN 190..232
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029800"
FT ACT_SITE 190
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_00664"
FT SITE 189..190
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_00664"
FT MOD_RES 190
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_00664"
SQ SEQUENCE 232 AA; 25472 MW; 2FE73B583D2BC83B CRC64;
MSLIDTVRNT LVPVHREGYR FIAIFFVVSL ALGFLWEPLM WIGFVLTAWC AYFFRDPERM
TPIDDDLVIS PADGTVSSVA TVMPPEELGL GSEPMLRISV FMNVFNCHVN RAPMGGTVRR
IAYRAGKFVN AELDKASQEN ERNGLVIETK HGQIGVVQIA GLVARRILCW TRESASLEAG
ERFGLIRFGS RLDVFLPAGA EPRVTVGQTA TGGETVLAEF GSAKGPVISR RA
