SAHH_HALWD
ID SAHH_HALWD Reviewed; 432 AA.
AC Q18EV6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563};
DE EC=3.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00563};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563};
DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563};
GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; OrderedLocusNames=HQ_3414A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-
CC Rule:MF_00563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
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DR EMBL; AM180088; CAJ53511.1; -; Genomic_DNA.
DR RefSeq; WP_011572608.1; NC_008212.1.
DR AlphaFoldDB; Q18EV6; -.
DR SMR; Q18EV6; -.
DR STRING; 362976.HQ_3414A; -.
DR EnsemblBacteria; CAJ53511; CAJ53511; HQ_3414A.
DR GeneID; 4193683; -.
DR KEGG; hwa:HQ_3414A; -.
DR eggNOG; arCOG04137; Archaea.
DR HOGENOM; CLU_025194_2_1_2; -.
DR OMA; NKYGCRE; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000001975; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 1.
DR HAMAP; MF_00563; AdoHcyase; 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; PTHR23420; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..432
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000260219"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 163..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 226..231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 305..307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 352
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
SQ SEQUENCE 432 AA; 46864 MW; DB9BBA686AC2774A CRC64;
MSAYSPLSAQ LDADTDVDVE STRTEGRRKM EWTLQHMPIL QELRARFAET KPLAGETIGM
AMHVEAKTAN LVELLALGGA EVAITGCNPL STHDDVSAAL DSNENVTSYA KRGVDEEAYY
DAIEAVVAHE PTITIDDGMD MVYAIHEDHP DLLDTIIGGA EETTTGVHRL RAMDEDDELQ
YPVFAVNDTP MKRLFDNVHG TGESALATIA MTTNLSYAGK NVVVAGYGYC GKGVAQKAAG
QNANVIVTEV EPRRALEAHM EGYEVMPMNE AATRGDVFVT TTGNRDVITQ EDFEVMSDGA
ILANAGHFDV EINLEELSEL AIDTYEARDG VQAYELGDGR RLNVLAEGRL VNLAAPIALG
HPAEVMDQSF GIQAVCVREL IENKSSYDAG VHNVPDELDR EVAEIKLKAE GVDIDSLTQT
QSEYLDSWSH GT
