ID A0A087CZ33_9BIFI Unreviewed; 457 AA.
AC A0A087CZ33;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000313|EMBL:KFI88533.1};
DE EC=3.3.1.1 {ECO:0000313|EMBL:KFI88533.1};
GN ORFNames=BREU_0654 {ECO:0000313|EMBL:KFI88533.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI88533.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI88533.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI88533.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI88533.1}.
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DR EMBL; JGZK01000001; KFI88533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087CZ33; -.
DR STRING; 1437610.BREU_0654; -.
DR eggNOG; COG0499; Bacteria.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; 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 PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR Pfam; PF05221; AdoHcyase; 2.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KFI88533.1};
KW NAD {ECO:0000256|PIRSR:PIRSR001109-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984}.
FT DOMAIN 207..366
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 239..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 360
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 457 AA; 48768 MW; C8E9FF26520414BC CRC64;
MAVETTCGRT GMAATSFRFD ADTPIDEIPD MRDATGLEAM AYAEAHMPVL HNVLSELQRE
GTDFTGVRIA VCLILEPKTA ILLRKLKAAG AIVGVYCGPD STDPRVAEQL RREGVIVESS
RDWTPEQAHD AALRLLDIIE PDIIIDDGAS FARLASLERP DLVANLIGVA EETTSGVRAF
AGMEAAGALT YPVVAVNDSI LKTGFDNAHG TGETCVTTMQ RILGDHAFEN ARVTVIGYGP
VGRGFARRVR ALGATVTVCD IDAVAALQAV FDGFAAQDID DALAEANIVV SATGVRHTIT
LDHLRLMHEG AVVAVIGGIA NEIALDEIPH FMPEVNRDSV ELHVPDGPTV TLLADGDGVN
YTVGGGNPIE IMDLSFAVQA SAVAYLLDHR GELPHHLIRL DAATDRRIAD AALKARGYRA
SHAVADNGYD WRLTRFEENA RHSATQPEAD TPATKEA
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