ID A0A0U5D1B4_9EURY Unreviewed; 202 AA.
AC A0A0U5D1B4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Putative archaetidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00664};
DE EC=4.1.1.- {ECO:0000256|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Archaetidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00664};
GN Name=psd {ECO:0000313|EMBL:CQH62306.1};
GN Synonyms=asd {ECO:0000256|HAMAP-Rule:MF_00664};
GN ORFNames=HHUB_3710 {ECO:0000313|EMBL:CQH62306.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH62306.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
CC -!- FUNCTION: Catalyzes the formation of archaetidylethanolamine (PtdEtn)
CC from archaetidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00664}.
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:0000256|HAMAP-
CC Rule:MF_00664};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00664};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00664};
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664};
CC Peripheral membrane protein {ECO:0000256|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:0000256|HAMAP-Rule:MF_00664}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-A subfamily. {ECO:0000256|HAMAP-Rule:MF_00664}.
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DR EMBL; LN831302; CQH62306.1; -; Genomic_DNA.
DR RefSeq; WP_059058026.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5D1B4; -.
DR STRING; 1407499.HHUB_3710; -.
DR GeneID; 26660297; -.
DR KEGG; hhb:Hhub_3710; -.
DR OrthoDB; 50255at2157; -.
DR Proteomes; UP000066737; Chromosome I.
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 NCBIfam; NF038088; anchor_synt_D; 1.
DR PANTHER; PTHR35809; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR PANTHER; PTHR35809:SF1; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00664}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00664};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00664};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_00664};
KW Reference proteome {ECO:0000313|Proteomes:UP000066737};
KW Zymogen {ECO:0000256|HAMAP-Rule:MF_00664}.
FT CHAIN 1..163
FT /note="Archaetidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT /id="PRO_5023256676"
FT CHAIN 164..202
FT /note="Archaetidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT /id="PRO_5023256675"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT SITE 163..164
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT MOD_RES 164
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ SEQUENCE 202 AA; 22201 MW; 3CBC300C19B3B641 CRC64;
MLARGSWKWT YALPAAVAGA ALLLVSSLWG VAALALAGFV VWFHRDPERT PEGRGVLTPA
DGKVSVARET DDGRLRVGVF MNVHDVHVNR APLAGTVEAV EHRDGGHRPA FDKESERNER
VRVTCDDYEV VLIAGAFARR IHPYVEPGDD LARGDRISHI SFGSRADVVL PREYDRDDLL
VENGEKVSAG ETVVARRSPN RE
//
