ASD_ARCFU
ID ASD_ARCFU Reviewed; 195 AA.
AC O28234;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Putative archaetidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664, ECO:0000305|PubMed:16243780};
DE EC=4.1.1.- {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_00664, ECO:0000305|PubMed:16243780};
GN OrderedLocusNames=AF_2045;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION IN ARCHAEAL LIPID BIOSYNTHESIS.
RX PubMed=16243780; DOI=10.1155/2005/452563;
RA Daiyasu H., Kuma K., Yokoi T., Morii H., Koga Y., Toh H.;
RT "A study of archaeal enzymes involved in polar lipid synthesis linking
RT amino acid sequence information, genomic contexts and lipid composition.";
RL Archaea 1:399-410(2005).
CC -!- FUNCTION: Catalyzes the formation of archaetidylethanolamine (PtdEtn)
CC from archaetidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00664,
CC ECO:0000305|PubMed:16243780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=archaetidylserine + H(+) = archaetidylethanolamine + CO2;
CC Xref=Rhea:RHEA:51488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:71517, ChEBI:CHEBI:134176; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00664, ECO:0000305|PubMed:16243780};
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 -!- 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 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 (By
CC similarity). {ECO:0000250|UniProtKB:B3L2V1,
CC ECO:0000250|UniProtKB:P0A8K1}.
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 ECO:0000305|PubMed:16243780}.
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DR EMBL; AE000782; AAB89201.1; -; Genomic_DNA.
DR PIR; D69505; D69505.
DR RefSeq; WP_010879537.1; NC_000917.1.
DR AlphaFoldDB; O28234; -.
DR SMR; O28234; -.
DR STRING; 224325.AF_2045; -.
DR EnsemblBacteria; AAB89201; AAB89201; AF_2045.
DR GeneID; 1485272; -.
DR KEGG; afu:AF_2045; -.
DR eggNOG; arCOG04470; Archaea.
DR HOGENOM; CLU_072492_1_0_2; -.
DR OMA; VSIFMSP; -.
DR OrthoDB; 105037at2157; -.
DR PhylomeDB; O28234; -.
DR Proteomes; UP000002199; 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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Cell membrane; Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Zymogen.
FT CHAIN 1..158
FT /note="Archaetidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029819"
FT CHAIN 159..195
FT /note="Archaetidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000029820"
FT ACT_SITE 159
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 158..159
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 159
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 195 AA; 21558 MW; 3FFBE5984581E5C3 CRC64;
MIERSGYGII AASLLLSAVA YLLHPLISAL FVGFALFTAY FFRDPERKIG EGVVSPADGR
IDYLEGRRLE IFMSPFDCHI NRAPWGGKVL SVKFIEGSTP PAFIRKSGVR TNEILIETEH
GVFRVLQMAG IFARRIVSYV SEGDVVKKGQ KIGMIRFGSR VVLEVPEGFR FVRGVGEKVK
AGETVALRDE SFQGS
