ID   ALMA1_EMIHU             Reviewed;         351 AA.
AC   P0DN21;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Dimethylsulfonioproprionate lyase 1 {ECO:0000305};
DE            Short=DMSP lyase 1 {ECO:0000305};
DE            EC=4.4.1.3 {ECO:0000269|PubMed:26113722};
DE   AltName: Full=Dimethylpropiothetin dethiomethylase 1 {ECO:0000305};
GN   Name=ALMA1 {ECO:0000303|PubMed:26113722};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND MUTAGENESIS OF
RP   CYS-108 AND CYS-265.
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
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. Constitutes by far the most highly
CC       expressed Alma gene in CCMP373 strain. {ECO:0000269|PubMed:26113722}.
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:0000269|PubMed:26113722};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26113722}.
CC   -!- INDUCTION: Highly expressed. {ECO:0000269|PubMed:26113722}.
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}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The smell of the sea - Issue
CC       174 of December 2015;
CC       URL="https://web.expasy.org/spotlight/back_issues/174/";
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DR   EMBL; KR703620; AKO62592.1; -; mRNA.
DR   AlphaFoldDB; P0DN21; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0047869; F:dimethylpropiothetin dethiomethylase activity; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Dimethylsulfonioproprionate lyase 1"
FT                   /id="PRO_0000433885"
FT   ACT_SITE        108
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:26113722"
FT   ACT_SITE        265
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:26113722"
FT   MUTAGEN         108
FT                   /note="C->A: Decreases dimethylsulfonioproprionate lyase
FT                   activity by a factor of 75."
FT                   /evidence="ECO:0000269|PubMed:26113722"
FT   MUTAGEN         265
FT                   /note="C->A: Abolishes dimethylsulfonioproprionate lyase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:26113722"
SQ   SEQUENCE   351 AA;  38006 MW;  8D7532D162A77222 CRC64;
     MGNCTSHPHH EPQVHFDTVD GMATVKAFAG IRQVTMGVLR IDYEYQTNLG DILDPRSFDF
     RIISATAEGL TFAKAKAGDK LDATGKELLE RAVRQLIDNG ADFIVGDCGF LVYWQVMVRD
     YAQDYAQKKY GRKCPVMMSS LVLALPLLAT IPSGGQIGIL TASEKSLQAV QKKLPIVIED
     HQKEDGGQRS RSVPAAEDPS GIMINFSDPR FKVVGLDEVK DFKHALDAQG ADAVNDRRDI
     AVQIAAYCQK VQEKNPQIAA WLIECTEAGG FAWAIKVGTG LPVWDPITLG RFLSLGFTAN
     VPNVALTLGQ HGENPLDPSA TTAGKGRCTG EEPGQIHALG AEFQAIREGT L