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
//