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Entry: L9ZQM5_9EURY
LinkDB: L9ZQM5_9EURY
Original site: L9ZQM5_9EURY 
ID   L9ZQM5_9EURY            Unreviewed;       427 AA.
AC   L9ZQM5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN   Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563};
GN   ORFNames=C484_15747 {ECO:0000313|EMBL:ELY88381.1};
OS   Natrialba taiwanensis DSM 12281.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1230458 {ECO:0000313|EMBL:ELY88381.1, ECO:0000313|Proteomes:UP000011648};
RN   [1] {ECO:0000313|EMBL:ELY88381.1, ECO:0000313|Proteomes:UP000011648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12281 {ECO:0000313|EMBL:ELY88381.1,
RC   ECO:0000313|Proteomes:UP000011648};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: May play a key role in the regulation of the intracellular
CC       concentration of adenosylhomocysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|PIRSR:PIRSR001109-2};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|PIRSR:PIRSR001109-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|RuleBase:RU004166}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY88381.1}.
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DR   EMBL; AOIL01000051; ELY88381.1; -; Genomic_DNA.
DR   RefSeq; WP_006826813.1; NZ_AOIL01000051.1.
DR   AlphaFoldDB; L9ZQM5; -.
DR   STRING; 1230458.C484_15747; -.
DR   PATRIC; fig|1230458.4.peg.3189; -.
DR   OrthoDB; 8479at2157; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000011648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000313|EMBL:ELY88381.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00563}.
FT   DOMAIN          192..353
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         158..160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         221..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         223..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         279
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         300..302
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         356
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   427 AA;  46641 MW;  7BC7A4BECD34A4CF CRC64;
     MSDYQRISEQ LDDVADAREE GRRKMDWAAQ HMPILEHVRD EFTADRPFEG ERIGMAMHVE
     AKTAMLVETL AEGGAEVAIT GCNPLSTHDD VSAALDAHEN ITSYAKRGVD DEEYYAAIEA
     VIGHEPTVTV DDGMDLVAAI HEDYPELIET IIGGAEETTT GVHRLRSMDD DGALEYPVFA
     VNDTPMKRLF DNVHGTGESS LASIAMTTNL SWAGKTVVVA GYGYCGKGVA KKASGQNANV
     IVTEVEPRRA LEAHMEGYEV MPMADAAEVG DVFLTTTGNR DVIVEEHFEK MQDGVLLANA
     GHFDIEIDLD ALADLSVDHY EARDGVDAYE MDDGRRLNVI AKGRLVNLAA PISLGHPVEV
     MDQSFGVQAA CVRELVDNGD QYDAGVHDVP DELDTEIAEI KLEAEGVEFD SLTETQREYM
     DSWDQGT
//
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