ID A0A1H3SSW6_9MICO Unreviewed; 392 AA.
AC A0A1H3SSW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:SDZ40641.1};
GN ORFNames=SAMN05216554_3627 {ECO:0000313|EMBL:SDZ40641.1};
OS Herbiconiux ginsengi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Herbiconiux.
OX NCBI_TaxID=381665 {ECO:0000313|EMBL:SDZ40641.1, ECO:0000313|Proteomes:UP000198891};
RN [1] {ECO:0000313|EMBL:SDZ40641.1, ECO:0000313|Proteomes:UP000198891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3491 {ECO:0000313|EMBL:SDZ40641.1,
RC ECO:0000313|Proteomes:UP000198891};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNPZ01000004; SDZ40641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3SSW6; -.
DR STRING; 381665.SAMN05216554_3627; -.
DR OrthoDB; 9802717at2; -.
DR Proteomes; UP000198891; Unassembled WGS sequence.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
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 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; 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:UP000198891}.
FT DOMAIN 175..336
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 206..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 330
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 392 AA; 41709 MW; F603A17BE6F6BEBB CRC64;
MTSDLAAQGA RRVEWIRSRM PLLAAMREEF ATRQPFAGHR IGMSLHIEPK TAVLLETLQA
GGAEIVSTGN HGSTQDDVVA FLREQGMTVF GARDDTLEQH HVNIAGVLDA AADMLLDNGG
DLAAGVVERG VTASILGGTE ETTSGGDRLR GELAGAIPFP VIVINDSLLK AIGENKHAVG
QSVVESFMRI TNLMVPGRRF VVVGYGWCGR GVAHYLRALG GKVAVVEVDE LKAFEAALDG
FRVSTAVDLA PWGDVFITAT GHADVLTLDA IERMHDGAVL ANCGHFPWEI DVAGLRDAAV
ASREIDDAIE RLDLADGRHV ILLAGGRMFN LAGREPKGNS LESMDLGFLL QTLSLERVAT
SAASLRAGAQ PVPDDIDRTI ARRMLAAMHA AE
//
