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Database: UniProt
Entry: A0A2G4I960_9BACT
LinkDB: A0A2G4I960_9BACT
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ID   A0A2G4I960_9BACT        Unreviewed;       303 AA.
AC   A0A2G4I960;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:PHX94970.1};
DE   Flags: Fragment;
GN   ORFNames=CK546_04910 {ECO:0000313|EMBL:PHX94970.1};
OS   Pedosphaera sp.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=2024890 {ECO:0000313|EMBL:PHX94970.1, ECO:0000313|Proteomes:UP000223988};
RN   [1] {ECO:0000313|EMBL:PHX94970.1, ECO:0000313|Proteomes:UP000223988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baikal-G1 {ECO:0000313|EMBL:PHX94970.1};
RX   PubMed=29079621;
RA   Cabello-Yeves P.J., Zemskaya T.I., Rosselli R., Coutinho F.H.,
RA   Zakharenko A.S., Blinov V.V., Rodriguez-Valera F.;
RT   "Genomes of novel microbial lineages assembled from the sub-ice waters of
RT   Lake Baikal.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:PHX94970.1}.
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DR   EMBL; NSHY01000113; PHX94970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4I960; -.
DR   Proteomes; UP000223988; 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; 1.
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; 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          61..223
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PHX94970.1"
SQ   SEQUENCE   303 AA;  33451 MW;  0AB6FDC18B20BB44 CRC64;
     LKSMSKKRGK GYWHGIVAAW KGVSEETTTG VHRLYQMLEQ GKLLVPAINV NDSVTKAKFD
     NLYGCRHSLV DGLNRAIDVM ISGKVAVICG YGDVGKGSAQ SLRGQGARVI VTEIDPICAL
     QAAMEGYEVT TLEDTLGRAD IYITTTGNKD ILTLEHMAKM KDQAVVANIG HFDNEIQVDR
     LNKAKGVKRK NIKPQVDQYT FADGHSIFML AEGRLVNLGC ATGHPSFVMS NSFSNQTLAQ
     LDLWANKDTY KVGVYRLSKK LDEEVARLHL EKIGVKLTRL TDKQAGYLGI SADGPYKPEH
     YRY
//
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