ID A0A2I3T4B4_PANTR Unreviewed; 543 AA.
AC A0A2I3T4B4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000084065.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000084065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2};
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR AlphaFoldDB; A0A2I3T4B4; -.
DR Ensembl; ENSPTRT00000092990.1; ENSPTRP00000084065.1; ENSPTRG00000051713.1.
DR GeneTree; ENSGT00950000182981; -.
DR Proteomes; UP000002277; Unplaced.
DR Bgee; ENSPTRG00000051713; Expressed in fibroblast and 20 other cell types or tissues.
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; 2.
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 NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 267..428
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 24..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
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 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 298..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 422
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 543 AA; 60439 MW; FFA4A298B3F6436A CRC64;
MLGSKKKYIV NGNSGIKAQI QFADQKQEFN KRPTKIGRRS LSRSISQSST DSYSSAASYT
DSSDDETSPR DKQQKNSKGS SDFCVKNIKQ AEFGRREIEI AEQEMPALMA LRKRAQGEKP
LAGAKIVGCT HITAQTAVLM ETLGALGAQC RWAACNIYST LNEVAAALAE SGFPVFAWKG
ESEDDFWWCI DRCVNVEGWQ PNMILDDGGD LTHWIYKKYP NMFKKIKGIV EESVTGVHRL
YQLSKAGKLC VPAMNVNDSV TKQKFDNLYC CRESILDGLK RTTDMMFGGK QVVVCGYGEV
GKGCCAALKA MGSIVYVTEI DPICALQACM DGFRLVKLNE VIRQVDIVIT CTGNKNVVTR
EHLDRMKNSC IVCNMGHSNT EIDVASLRTP ELTWERVRSQ VDHVIWPDGK RIVLLAEGRL
LNLSCSTVPT FVLSITATTQ ALALIELYNA PEGRYKQDVY LLPKKMDEYV ASLHLPTFDA
HLTELTDEQA KYLGLNKNGP FKPNYYRCLG LPRNQGHLGS DELPALELVF ASPTTYAYMN
SEK
//