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Database: UniProt
Entry: A0A087R8I1_APTFO
LinkDB: A0A087R8I1_APTFO
Original site: A0A087R8I1_APTFO 
ID   A0A087R8I1_APTFO        Unreviewed;       454 AA.
AC   A0A087R8I1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE            EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
DE   Flags: Fragment;
GN   ORFNames=AS27_08682 {ECO:0000313|EMBL:KFM09785.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09785.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM09785.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09785.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL226211; KFM09785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087R8I1; -.
DR   STRING; 9233.A0A087R8I1; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000053286; 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: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:UP000053286}.
FT   DOMAIN          212..373
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         243..248
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         367
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM09785.1"
FT   NON_TER         454
FT                   /evidence="ECO:0000313|EMBL:KFM09785.1"
SQ   SEQUENCE   454 AA;  50557 MW;  C8C999534C648093 CRC64;
     AASYTDSSDD ETSPRDKQQK NSKGSSDFCV KNIKQAEFGR REIEIAEQEM PALMALRKRA
     QGEKPLAGAK IVGCTHITAQ TAVLMETLGA LGAQCRWAAC NIYSTLNEVA AALAESGFPV
     FAWKGESEDD FWWCIDRCVN VEGWQPNMIL DDGGDLTHWI YKKYPNMFKK IKGIVEESVT
     GVHRLYQLSK AGKLCVPAMN VNDSVTKQKF DNLYCCRESI LDGLKRTTDM MFGGKQVVVC
     GYGEVGKGCC AALKAMGSIV YVTEIDPICA LQACMDGFRL VKLNEVIRQV DIVITCTGNK
     NVVTREHLDR MKNSCIVCNM GHSNTEIDVA SLRTPELTWE RVRSQVDHVI WPDGKRIVLL
     AEGRLLNLSC STVPTFVLSI TATTQASRAL ALIELYNAPE GRYKQDVYLL PKKMDEYVAS
     LHLPTFDAHL TELTDEQAKY LGLNKNGPFK PNYY
//
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