ID   ALM1_EMIHU              Reviewed;         351 AA.
AC   R1F9H0;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Dimethylsulfonioproprionate lyase 1 {ECO:0000305};
DE            Short=DMSP lyase 1 {ECO:0000305};
DE            EC=4.4.1.3 {ECO:0000250|UniProtKB:P0DN21};
DE   AltName: Full=Dimethylpropiothetin dethiomethylase 1 {ECO:0000305};
GN   Name=ALMA1 {ECO:0000303|PubMed:26113722};
GN   ORFNames=EMIHUDRAFT_99026 {ECO:0000312|EMBL:EOD32021.1};
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:P0DN21}.
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   -!- MISCELLANEOUS: At least 10 million metric tons of volatile dimethyl
CC       sulfide (DMS) are released into the atmosphere annually by the
CC       dimethylsulfonioproprionate lyase in oceans. It is a component of the
CC       tangy aroma of the seaside and functions as a chemical attractant that
CC       guides various marine animals, such as sea birds, invertebrates, and
CC       some mammals, toward potential food supplies. DMS oxidation products
CC       act as condensation nuclei, causing water molecules to coalesce, with
CC       possible effects on local climate through enhanced cloud formation.
CC       {ECO:0000305|PubMed:26113722}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; KB864557; EOD32021.1; -; Genomic_DNA.
DR   RefSeq; XP_005784450.1; XM_005784393.1.
DR   AlphaFoldDB; R1F9H0; -.
DR   GeneID; 17277293; -.
DR   KEGG; ehx:EMIHUDRAFT_99026; -.
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..351
FT                   /note="Dimethylsulfonioproprionate lyase 1"
FT                   /id="PRO_0000433886"
FT   ACT_SITE        108
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0DN21"
FT   ACT_SITE        265
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0DN21"
SQ   SEQUENCE   351 AA;  37997 MW;  9EE8894B064DBECF CRC64;
     MGNCTSHPHH EPQVHFDTVD GMATVKAFAG IRQVTMGVLR IDYEYQTNLG DILDPRSFDF
     RIISATAEGL TFAKAKAGDK LDATGKELLE RAVRQLIDNG ADFIVGDCGF LVYWQVMVRD
     YAQDYAQKKY GRKCPVMMSS LVLALPLLAT IPSGGQIGIL TASEKSLQAV QKKLPIVIED
     QQKEDGGQRS RSVPAAEDPS GIMINFSDPR FKVVGLDEVK DFKHALDAQG ADAVNDRRDI
     AVQIAAYCQK VQEKNPQIAA WLIECTEAGG FAWAIKVGTG LPVWDPITLG RFLSLGFTAN
     VPNVALTLGQ HGENPLDPSA TTAGKGRCTG EEPGQIHALG AEFQAIREGT L