ID I3D297_9ARCH Unreviewed; 417 AA.
AC I3D297;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:EIJ65840.1};
DE EC=3.3.1.1 {ECO:0000313|EMBL:EIJ65840.1};
GN Name=ahcY_1 {ECO:0000313|EMBL:EIJ65840.1};
GN ORFNames=BD31_I0179 {ECO:0000313|EMBL:EIJ65840.1};
OS Candidatus Nitrosopumilus salaria BD31.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=859350 {ECO:0000313|EMBL:EIJ65840.1, ECO:0000313|Proteomes:UP000003423};
RN [1] {ECO:0000313|EMBL:EIJ65840.1, ECO:0000313|Proteomes:UP000003423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD31 {ECO:0000313|EMBL:EIJ65840.1,
RC ECO:0000313|Proteomes:UP000003423};
RX PubMed=22461555; DOI=10.1128/JB.00013-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome sequence of "Candidatus Nitrosopumilus salaria" BD31, an ammonia-
RT oxidizing archaeon from the San Francisco Bay estuary.";
RL J. Bacteriol. 194:2121-2122(2012).
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, ECO:0000256|RuleBase:RU004166}.
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:EIJ65840.1}.
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DR EMBL; AEXL02000090; EIJ65840.1; -; Genomic_DNA.
DR AlphaFoldDB; I3D297; -.
DR PATRIC; fig|859350.6.peg.1106; -.
DR Proteomes; UP000003423; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; 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 NCBIfam; TIGR00936; ahcY; 1.
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:EIJ65840.1};
KW NAD {ECO:0000256|PIRSR:PIRSR001109-2}.
FT DOMAIN 188..349
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 219..224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 417 AA; 46267 MW; E03B302386CAD52A CRC64;
MEELLSKVKT SSKLVQEGKL SYQWARSHMQ ILDNTINRFK KSKPLKGVTL GFCLHITKET
SVLLMGAKEL GATVACCGGN PLTTQDNIAA FLASQGIHVY AWHGQSVKEY DWCIDQVLKH
KPTILTDDGA DMNIKAHFDK RFSTMKILGA TEETTAGVTR IRAVENQGKL RYPVILVNEA
YTKHMFDNRY GTGQSTIDGY LRGMNLLMAS KRVVVVGYGW VGRGVASRFH GMGSKVIVTE
VDPIKALEAH MDGFEVMPMS QAAKIGDMFV TCTGMTSVIR KEHILQMKNG AIMGNVGHFD
VEIDSKFLLK SSKSVKEVRP NLDECTLKNG KVVYLIGQGR LANLVAAEGH PPEVMAQSFS
NQILSVLYIL KNHKKMENKI INVPEEIDKQ VAVDALNAMN VKIDKLTSEQ IKYANSW
//
