ID F6RMS6_CALJA Unreviewed; 512 AA.
AC F6RMS6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Adenosylhomocysteinase like 2 {ECO:0000313|Ensembl:ENSCJAP00000019122.4};
GN Name=AHCYL2 {ECO:0000313|Ensembl:ENSCJAP00000019122.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000019122.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000019122.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000019122.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; F6RMS6; -.
DR Ensembl; ENSCJAT00000020201.4; ENSCJAP00000019122.4; ENSCJAG00000010323.5.
DR GeneTree; ENSGT00950000182981; -.
DR Proteomes; UP000008225; Chromosome 8.
DR Bgee; ENSCJAG00000010323; Expressed in kidney and 6 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; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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:UP000008225}.
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 512 AA; 57236 MW; F77816C0C11833D0 CRC64;
MEQWDGNEGT SAFHMPEWMI 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 FKPNYYRKAI AA
//
