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Database: UniProt
Entry: A0A1A9ZFM3_GLOPL
LinkDB: A0A1A9ZFM3_GLOPL
Original site: A0A1A9ZFM3_GLOPL 
ID   A0A1A9ZFM3_GLOPL        Unreviewed;       501 AA.
AC   A0A1A9ZFM3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, 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};
OS   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI013094-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI013094-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI013094-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   AlphaFoldDB; A0A1A9ZFM3; -.
DR   STRING; 7398.A0A1A9ZFM3; -.
DR   EnsemblMetazoa; GPAI013094-RA; GPAI013094-PA; GPAI013094.
DR   VEuPathDB; VectorBase:GPAI013094; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000092445; Unassembled WGS sequence.
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: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}.
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;  55736 MW;  510DB847A5732249 CRC64;
     MQKINSDAPV CDLGFNEKHE AIQPEALKIA SKSRRRSSAA STCSFSSACF TGSSDEDDIS
     PREKRQCNSR GYTDFCVKNV INHHAFGRRE IEIAEQEMPG IMTLRRRAGD DKPLKKANIV
     GCTHINAQTA VLIETLIKLG ASVRWAACNI YSTQNAVAAA LAEVNVPIFA WRGETEEDFW
     WCLDNCVNAD GWQPNMILDD GGDATHLMWK KYPELFKGIK GIVEESITGV HRLYHMSKTG
     KLSVPAINVN DSVTKMKFDN FYSIRESILD SLKRATDVLF GGKQVVVCGY GDVGKGCAKG
     LRAQGCIVYV TEIDPICALQ ASMDGFRVVK LNEVIRNVDI VVTATGNKHV VTREHMDRLK
     HGCIVCNMGH SNSEIDINSL HTPELSWERV RSQVDHIFWP DGKMMVLLAE GRLVNLSCST
     IPSFVVSVTA SAQALALIEL YNAVPGRYKS DVYLLPKKMD EYVSSLHLPT FDAHLTELTD
     EQAKYLGLNK AGPFKPNYYR Y
//
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