ID A3CT79_METMJ Unreviewed; 408 AA.
AC A3CT79;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=S-inosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE Short=SIHH {ECO:0000256|HAMAP-Rule:MF_00563};
DE EC=3.13.1.9 {ECO:0000256|HAMAP-Rule:MF_00563};
GN OrderedLocusNames=Memar_0646 {ECO:0000313|EMBL:ABN56579.1};
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN56579.1, ECO:0000313|Proteomes:UP000002146};
RN [1] {ECO:0000313|EMBL:ABN56579.1, ECO:0000313|Proteomes:UP000002146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1
RC {ECO:0000313|Proteomes:UP000002146};
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of S-inosyl-L-homocysteine (SIH) to
CC L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L-
CC methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH)
CC produced from SAM-dependent methylation reactions. Can also catalyze
CC the reverse reaction in vitro, i.e. the synthesis of SIH from Hcy and
CC inosine. {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-inosyl-L-homocysteine = inosine + L-homocysteine;
CC Xref=Rhea:RHEA:59828, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:57985, ChEBI:CHEBI:58199; EC=3.13.1.9;
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; S-adenosyl-L-methionine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- MISCELLANEOUS: SAH is a product of SAM methyltransferases and is known
CC to be a feedback inhibitor of these enzymes. As a result of this
CC inhibition, organisms have evolved efficient enzymes to metabolize SAH
CC via different pathways. The pathway found in methanogens differs from
CC the canonical pathway, it uses the deamination of S-adenosyl-L-
CC homocysteine to form S-inosyl-L-homocysteine for the regeneration of
CC SAM from S-adenosyl-L-homocysteine. {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}.
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DR EMBL; CP000562; ABN56579.1; -; Genomic_DNA.
DR RefSeq; WP_011843490.1; NC_009051.1.
DR AlphaFoldDB; A3CT79; -.
DR STRING; 368407.Memar_0646; -.
DR GeneID; 76731216; -.
DR KEGG; mem:Memar_0646; -.
DR eggNOG; arCOG04137; Archaea.
DR HOGENOM; CLU_025194_0_2_2; -.
DR OrthoDB; 8479at2157; -.
DR UniPathway; UPA00315; -.
DR Proteomes; UP000002146; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016802; F:trialkylsulfonium hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 2.
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; 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:ABN56579.1};
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 175..334
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 141..143
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 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 204..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 206..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 227
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 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 283..285
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 328
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 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 408 AA; 44201 MW; 287B81774EA8B3DE CRC64;
MESGDLKIAW ARQYMPVLSS IRKRFVEEKP FSGMTIGMAL HVEAKTAVLV ETLAAGGAEV
HITGCNPLST QDDVATALDT REGIHSYARR GASVEEYYAA IDRVLDARPA ITIDDGMDLI
FRIHTERRDV LDSVIGGCEE TTTGIHRLRA MAQEGALRFP VVAVNDTPMK HFFDNVHGTG
ESSLASIMIT TNILIAGKRF VVAGYGYCGR GLAQKARSLG ARVIVTEVDP RRALQAHMDG
FEVMTMDDAT HLGDIFVTTT GNTSILTERH FPKMKDGAIL ANAGHFNVEI DVDWLAAHAD
STVHRDGVDT YVLDGKAVHV LAEGRLVNLA TPKGMGHPVE VMDLSFAVQA LSAEFIAKHG
RELAPGVHDV PSAIDEGVAR LKLDALGLSI DRLTPDQETY MSSWTIGT
//
