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Database: UniProt
Entry: A0A1S3FG68_DIPOR
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ID   A0A1S3FG68_DIPOR        Unreviewed;       404 AA.
AC   A0A1S3FG68;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE            EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN   Name=Ahcyl2 {ECO:0000313|RefSeq:XP_012875491.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012875491.1};
RN   [1] {ECO:0000313|RefSeq:XP_012875491.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012875491.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_012875491.1; XM_013020037.1.
DR   AlphaFoldDB; A0A1S3FG68; -.
DR   SMR; A0A1S3FG68; -.
DR   STRING; 10020.ENSDORP00000012772; -.
DR   GeneID; 105988404; -.
DR   KEGG; dord:105988404; -.
DR   CTD; 23382; -.
DR   InParanoid; A0A1S3FG68; -.
DR   OMA; HIIWPDA; -.
DR   OrthoDB; 120477at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:RHEA.
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   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:SF2; ADENOSYLHOMOCYSTEINASE 3; 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:UP000081671}.
FT   DOMAIN          163..324
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         128
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         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         194..199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         215
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   404 AA;  45055 MW;  18B84A57A63770B6 CRC64;
     MPALMALRKR AQGEKPLAGA KIVGCTHITA QTAVLMETLG ALGAQCRWAA CNIYSTLNEV
     AAALAESGFP VFAWKGESED DFWWCIDRCV NVEGWQPNMI LDDGGDLTHW IYKKYPNMFK
     KIKGIVEESV TGVHRLYQLS KAGKLCVPAM NVNDSVTKQK FDNLYCCRES ILDGLKRTTD
     MMFGGKQVVV CGYGEVGKGC CAALKAMGSI VYVTEIDPIC ALQACMDGFR LVKLNEVIRQ
     VDIVITCTGN KNVVTREHLD RMKNSCIVCN MGHSNTEIDV ASLRTPELTW ERVRSQVDHV
     IWPDGKRIVL LAEGRLLNLS CSTVPTFVLS ITATTQALAL IELYNAPEGR YKQDVYLLPK
     KMDEYVASLH LPTFDAHLTE LTDEQAKYLG LNKNGPFKPN YYRY
//
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