PISD_RAT
ID PISD_RAT Reviewed; 406 AA.
AC D3ZAW2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:6862014};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Flags: Precursor;
GN Name=Pisd {ECO:0000255|HAMAP-Rule:MF_03208};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=6862014; DOI=10.1016/0014-5793(83)81141-7;
RA Zborowski J., Dygas A., Wojtczak L.;
RT "Phosphatidylserine decarboxylase is located on the external side of the
RT inner mitochondrial membrane.";
RL FEBS Lett. 157:179-182(1983).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=2618245;
RA Dygas A., Zborowski J.;
RT "Effect of triton X-100 on the activity and solubilization of rat liver
RT mitochondrial phosphatidylserine decarboxylase.";
RL Acta Biochim. Pol. 36:131-141(1989).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Plays a central role in phospholipid
CC metabolism and in the interorganelle trafficking of phosphatidylserine.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245}.
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_03208, ECO:0000269|PubMed:2618245};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine.
CC {ECO:0000269|PubMed:2618245}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for phosphatidylserine {ECO:0000269|PubMed:2618245};
CC Vmax=77 nmol/h/mg enzyme {ECO:0000269|PubMed:2618245};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:2618245};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis. {ECO:0000305|PubMed:2618245}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:6862014}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:6862014}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014};
CC Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:6862014}. Note=Anchored to the mitochondrial inner
CC membrane through its interaction with the integral membrane beta chain.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:6862014}.
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. 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 an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; AC105515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZAW2; -.
DR SMR; D3ZAW2; -.
DR STRING; 10116.ENSRNOP00000024812; -.
DR PaxDb; D3ZAW2; -.
DR PeptideAtlas; D3ZAW2; -.
DR PRIDE; D3ZAW2; -.
DR RGD; 1596729; Pisd.
DR VEuPathDB; HostDB:ENSRNOG00000018319; -.
DR eggNOG; KOG2420; Eukaryota.
DR HOGENOM; CLU_029061_3_0_1; -.
DR InParanoid; D3ZAW2; -.
DR OMA; AIEWQLH; -.
DR TreeFam; TF313148; -.
DR UniPathway; UPA00558; -.
DR PRO; PR:D3ZAW2; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000018319; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; D3ZAW2; baseline and differential.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Pyruvate; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Zymogen.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 50..406
FT /note="Phosphatidylserine decarboxylase proenzyme,
FT mitochondrial"
FT /id="PRO_0000435574"
FT CHAIN 50..374
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435575"
FT CHAIN 375..406
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435576"
FT TOPO_DOM 50..60
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:6862014"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 80..406
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:6862014"
FT ACT_SITE 188
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 264
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 375
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 375
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 374..375
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 375
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
SQ SEQUENCE 406 AA; 45824 MW; 5358A6A2A6D72EE7 CRC64;
MAVAGGRGCV RSLREGVLWR SSPCHCDYTA TRHFLGALQK LPLQAWVRKV HTAPLRTLFL
LRPVPILLAA GGGYAGYRQY EKYRERQLEK LGLEIPPKLA SHWEVSLYKS VPTRLLSRAC
GRLNQVELPS WLRRPVYSLY IWTFGVNMTE AAVEDLQHYR NLSEFFRRKL KPQARPVCGL
HSVISPSDGK ILTFGQVKNS EVEQVKGVTY SLESFLGPRA CTEDLPFPPA SSCDSFRNQL
VTREGNELYH CVIYLAPGDY HCFHSPTDWT VSHRRHFPGS LMSVNPGMAR WIKELFCHNE
RVVLTGDWKH GFFSLTAVGA TNVGSIRIHF DQDLHTNSPS YSKGSYNDLS FVTHANKEGI
PMRKGEPLGE FNLGSTIVLI FEAPKDFNFR LKAGQKILFG EALGSL
