ID K0B4B2_9ARCH Unreviewed; 413 AA.
AC K0B4B2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:AFS80978.1};
GN ORFNames=NKOR_05460 {ECO:0000313|EMBL:AFS80978.1};
OS Candidatus Nitrosopumilus koreensis AR1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229908 {ECO:0000313|EMBL:AFS80978.1, ECO:0000313|Proteomes:UP000006101};
RN [1] {ECO:0000313|EMBL:AFS80978.1, ECO:0000313|Proteomes:UP000006101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR1 {ECO:0000313|EMBL:AFS80978.1,
RC ECO:0000313|Proteomes:UP000006101};
RX PubMed=23209206; DOI=10.1128/JB.01857-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Kwon K., Lee J.H.,
RA Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus koreensis" AR1, from Marine Sediment.";
RL J. Bacteriol. 194:6940-6941(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}.
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DR EMBL; CP003842; AFS80978.1; -; Genomic_DNA.
DR RefSeq; WP_014963363.1; NC_018655.1.
DR AlphaFoldDB; K0B4B2; -.
DR STRING; 1229908.NKOR_05460; -.
DR GeneID; 13725128; -.
DR KEGG; nkr:NKOR_05460; -.
DR PATRIC; fig|1229908.8.peg.1191; -.
DR HOGENOM; CLU_025194_2_1_2; -.
DR Proteomes; UP000006101; Chromosome.
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 NAD {ECO:0000256|PIRSR:PIRSR001109-2}.
FT DOMAIN 184..345
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 179
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 215..220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 413 AA; 45827 MW; A603C57E7229A6A3 CRC64;
MSKVKSSPKL IKEGKLSYEW ARSHMQILDN TINRFKKSKP LKGITLGFCL HITKETSVLL
IGAKELGANV ACCGGNPLTT QDNIAAFLAS QGIHVYAWNG QSVKDYDWCI DQVLKHKPTI
LTDDGADMNI KAHFDKRFKN MNILGATEET TAGVTRIRAV ENQGKLRYPV ILVNEAYTKH
MFDNRYGTGQ STIDGYLRAM NLLMASKRVV VVGYGWVGRG VASRCHGMGS KVIVTEIDPI
KALEAHMDGF EVMPMAQAAK LGDIFITCTG MTSVIRKEHI LKMKDGAIMG NVGHFDVEID
SEFLLKKSKS VKEVRPSLDE CVLKNGKKVY LIGQGRLANL VAAEGHPPEV MAQSFSNQIL
SVMYILKNHK KMEKKIINVP QEIDTQVAVD ALKAMDVKID KLTPEQVKYA NSW
//