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Database: UniProt
Entry: A0A1I8MJ65_MUSDO
LinkDB: A0A1I8MJ65_MUSDO
Original site: A0A1I8MJ65_MUSDO 
ID   A0A1I8MJ65_MUSDO        Unreviewed;       501 AA.
AC   A0A1I8MJ65;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE            EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN   Name=101890828 {ECO:0000313|EnsemblMetazoa:MDOA005450-PA};
GN   Synonyms=LOC101890828 {ECO:0000313|RefSeq:XP_005182074.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA005450-PA};
RN   [1] {ECO:0000313|EnsemblMetazoa:MDOA005450-PA}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA005450-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005182074.1}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|RefSeq:XP_005182074.1};
RG   RefSeq;
RL   Submitted (NOV-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_005182074.1; XM_005182017.3.
DR   STRING; 7370.A0A1I8MJ65; -.
DR   EnsemblMetazoa; MDOA005450-RA; MDOA005450-PA; MDOA005450.
DR   GeneID; 101890828; -.
DR   KEGG; mde:101890828; -.
DR   VEuPathDB; VectorBase:MDOA005450; -.
DR   eggNOG; KOG1370; Eukaryota.
DR   OrthoDB; 120477at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
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   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:UP000694905}.
FT   DOMAIN          260..421
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         291..296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         312
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         415
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   501 AA;  55811 MW;  281DEC02BA73212D CRC64;
     MNRNIETPIC DLGFSDKQEA VQPEALKLAS RTRRRSSAAS TCSFSSACFT ASSDEDTVIS
     PREKKQRNTK GFTDFCVKNV LSQHGFGRRE IEIAEQEMPG IMTLRKRARE DKPLRNANIV
     CCTHINAQTA VMVEGLIELG ASVRWASCNI YSTQNAVAAA LAEAGIPVFA WRGETEEDFW
     WCLDKCINAP GWAPNMILDD GGDATHLMWK KYPEIFKGIK GIVEESLTGV HRLYHMSKNG
     KLTVPAINVN DSVTKMKFDN FYCVQDSILD SLKRSTDIMF GGKQVVVCGY GDVGKGCAKS
     LKAQGCIVYV TEIDPICALQ ASMDGHRVVT LNEVIRNVDI VVTATGNKNI VTREHMNRMK
     NGCIVCNMGH SNSEIDVNSL HTPELTWERV RSQVDHIIWP DGRMIILLAE GRLVNMSCST
     IPSFVVSITA STQALALIEL YNAIPGRYKN DVYLLPKKMD EYVASLHLPT FDAHLTELTD
     EQAKYLGLNK SGPFKPNYYR Y
//
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