ID E3LMU2_CAERE Unreviewed; 437 AA.
AC E3LMU2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN Name=Cre-ahcy-1 {ECO:0000313|EMBL:EFP03304.1};
GN ORFNames=CRE_28195 {ECO:0000313|EMBL:EFP03304.1}, FL81_17044
GN {ECO:0000313|EMBL:POM30382.1}, FL82_12410
GN {ECO:0000313|EMBL:OZF74986.1}, GCK72_001866
GN {ECO:0000313|EMBL:KAF1770049.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|EMBL:EFP03304.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFP03304.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POM30382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM30382.1};
RX PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Reproductive Mode and the Evolution of Genome Size and Structure in
RT Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005323-e1005323(2015).
RN [4] {ECO:0000313|EMBL:POM30382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM30382.1};
RX PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Correction: Reproductive Mode and the Evolution of Genome Size and
RT Structure in Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005497-e1005497(2015).
RN [5] {ECO:0000313|EMBL:OZF74986.1, ECO:0000313|Proteomes:UP000216624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX439 {ECO:0000313|EMBL:OZF74986.1,
RC ECO:0000313|Proteomes:UP000216624};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:POM30382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PX356 {ECO:0000313|EMBL:POM30382.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:KAF1770049.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1770049.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1770049.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|RuleBase:RU000548}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR EMBL; DS268411; EFP03304.1; -; Genomic_DNA.
DR EMBL; WUAV01000001; KAF1770049.1; -; Genomic_DNA.
DR EMBL; NMWX01000912; OZF74986.1; -; Genomic_DNA.
DR EMBL; LFJK02001458; POM30382.1; -; Genomic_DNA.
DR RefSeq; XP_003115169.1; XM_003115121.1.
DR AlphaFoldDB; E3LMU2; -.
DR STRING; 31234.E3LMU2; -.
DR EnsemblMetazoa; CRE28195.1; CRE28195.1; WBGene00056188.
DR GeneID; 9815438; -.
DR KEGG; crq:GCK72_001866; -.
DR CTD; 9815438; -.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_0_1; -.
DR OMA; YIGVTVE; -.
DR OrthoDB; 120477at2759; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000216624; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome i.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
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 Hydrolase {ECO:0000256|RuleBase:RU000548};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000548};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 193..354
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 159..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 224..229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 348
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 355
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 437 AA; 47431 MW; 46A29103DCB7BA24 CRC64;
MAQSKPAYKV ADISLAEFGR KEITLAENEM PGLMAMRAKY GPTQPLKGAK IAGCLHMTIQ
TAVLIETLTA LGAEVQWSSC NIFSTQDHAA AAIAKTGVPV YAWKGETDEE YEWCIEQTIV
FKDGQPLNMI LDDGGDLTNL VHAKYSQYLP GIRGLSEETT TGVHNLAKML AKGDLKIPAI
NVNDSVTKSK FDNLYGIRES LPDGIKRATD VMLAGKVAVV AGYGDVGKGS AASLKAFGSR
VIVTEIDPIN ALQAAMEGYE VTTLEEAAPK ANIIVTTTGC KDIVTGKHFE LLPNDAIVCN
VGHFDCEIDV KWLNANATKK DTIKPQVDRY TLKNGRHIIL LAEGRLVNLG CATGHPSFVM
SNSFTNQVLA QVELWTKFGT PQEYKLGLYV LPKSLDEEVA ALHLEKLGVK LTKLSDEQAA
YLGVPIAGPY KPDHYRY
//
