ID   ALM2_EMIHU              Reviewed;         353 AA.
AC   R1DS73;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Dimethylsulfonioproprionate lyase 2 {ECO:0000250|UniProtKB:P0DN23};
DE            Short=DMSP lyase 2 {ECO:0000250|UniProtKB:P0DN23};
DE            EC=4.4.1.3 {ECO:0000250|UniProtKB:P0DN23};
DE   AltName: Full=Dimethylpropiothetin dethiomethylase 2 {ECO:0000250|UniProtKB:P0DN23};
GN   Name=ALMA2 {ECO:0000303|PubMed:26113722};
GN   ORFNames=EMIHUDRAFT_437551 {ECO:0000312|EMBL:EOD11554.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1516;
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=26113722; DOI=10.1126/science.aab1586;
RA   Alcolombri U., Ben-Dor S., Feldmesser E., Levin Y., Tawfik D.S., Vardi A.;
RT   "Identification of the algal dimethyl sulfide-releasing enzyme: A missing
RT   link in the marine sulfur cycle.";
RL   Science 348:1466-1469(2015).
CC   -!- FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into
CC       dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which
CC       sulfur is transported from oceans to the atmosphere and is a key
CC       component of the ocean sulfur cycle. {ECO:0000250|UniProtKB:P0DN23}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S,S-dimethyl-beta-propiothetin = acrylate + dimethyl sulfide +
CC         H(+); Xref=Rhea:RHEA:19965, ChEBI:CHEBI:15378, ChEBI:CHEBI:16457,
CC         ChEBI:CHEBI:17437, ChEBI:CHEBI:37080; EC=4.4.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P0DN21};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0DN21}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; KB868012; EOD11554.1; -; Genomic_DNA.
DR   RefSeq; XP_005763983.1; XM_005763926.1.
DR   AlphaFoldDB; R1DS73; -.
DR   GeneID; 17257733; -.
DR   KEGG; ehx:EMIHUDRAFT_437551; -.
DR   HOGENOM; CLU_786270_0_0_1; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0047869; F:dimethylpropiothetin dethiomethylase activity; IEA:UniProtKB-EC.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..353
FT                   /note="Dimethylsulfonioproprionate lyase 2"
FT                   /id="PRO_0000433889"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0DN21"
FT   ACT_SITE        274
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0DN21"
SQ   SEQUENCE   353 AA;  37891 MW;  A114FC809400FE7B CRC64;
     MGSASSKTRK DKAKSSTIAA CPTDTAAAKA CPTRLDDGLA QVAMFAGLRQ VTMGVLRIDY
     DYQTNLGDIL DPRSFDFRLV SATVEGLTFK RAQEGEPLPC YVMSNLDGAV KKLIDAGADF
     IVGDCGFLVY WQVYVRDFAQ QYAGGRACPV MLSSLVLSLP LLATIPVGGK IGILTASKGS
     LMKMQKKLAS VIELQKEEAR TRAVPAAVQP SGIEINFSDP RFKVVGLDTV NSFKTALADD
     SGVDDRRSIA IEIAKYCKQV ACEDPAICAW LIECTEAGGF SWAIKLGTGL PVWDPVTIGR
     FLSLGFTSSL PSVALTLGET GQVALDPNET DVSKGRPTKA EHRFGPEFEE MLQ