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Database: UniProt
Entry: A0A1Y2T3H6_SYMTR
LinkDB: A0A1Y2T3H6_SYMTR
Original site: A0A1Y2T3H6_SYMTR 
ID   A0A1Y2T3H6_SYMTR        Unreviewed;       334 AA.
AC   A0A1Y2T3H6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:OTA40879.1};
DE   Flags: Fragment;
GN   ORFNames=A6D92_12270 {ECO:0000313|EMBL:OTA40879.1};
OS   Symbiobacterium thermophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=2734 {ECO:0000313|EMBL:OTA40879.1, ECO:0000313|Proteomes:UP000194267};
RN   [1] {ECO:0000313|Proteomes:UP000194267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antunes L.P., Martins L.F., Pereira R.V., Thomas A.M., Barbosa D.,
RA   Nascimento L., Silva G.M., Condomitti G.W., Digiampietri L.A.,
RA   Lombardi K.C., Ramos P.L., Quaggio R.B., Oliveira J.C., Pascon R.C.,
RA   Cruz J.B., Silva A.M., Setubal J.C.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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:OTA40879.1}.
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DR   EMBL; LWLV01001063; OTA40879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2T3H6; -.
DR   Proteomes; UP000194267; Unassembled WGS sequence.
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; 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; 2.
DR   Pfam; PF00670; AdoHcyase_NAD; 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};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT   DOMAIN          190..334
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   NON_TER         334
FT                   /evidence="ECO:0000313|EMBL:OTA40879.1"
SQ   SEQUENCE   334 AA;  36062 MW;  6899C585E365FB1F CRC64;
     MPSKVSASTL RDPALAPSGH QKIDWVRAHM PILNQLEREL GEKKPLAGQR VAMSIHLEAK
     TAYMALVFAA AGAEVFLTGS NPLSTQDDVA AAVAERGVTV HAWRGATPAE YREHLIRTLE
     AARPTLLLDD GGDLTHLLHT SHADLAADLI GGSEETSTGV QRLRAMEAEG VLRFPMVAVN
     NARMKHLFDN RYGTGQSTLE SIMRNTNLSI AGKRVVVAGY GWCGKGVAMR ARGLGARVIV
     CEVDPVRANE ALMDGFEVMP MARAAALGDI FITVTGCEKV IRGEHFAVMR DGAILANAGH
     FDVEIWKPDL EAFGGKPVRV RPNVDQYTAP DGRR
//
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