ID   SAHH_CORGL              Reviewed;         474 AA.
AC   Q8NSC4;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-SEP-2026, entry version 135.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563};
DE            EC=3.13.2.1 {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}; Synonyms=sahH;
GN   OrderedLocusNames=Cgl0752, cg0860;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC
OS   11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 /
OS   534).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 /
RC   LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 /
RC   LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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=S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAF19456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB98145.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19456.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8NSC4; -.
DR   SMR; Q8NSC4; -.
DR   STRING; 196627.cg0860; -.
DR   PaxDb; 196627-cg0860; -.
DR   KEGG; cgb:cg0860; -.
DR   KEGG; cgl:Cgl0752; -.
DR   PATRIC; fig|196627.13.peg.736; -.
DR   eggNOG; COG0499; Bacteria.
DR   HOGENOM; CLU_025194_2_1_11; -.
DR   OrthoDB; 9802717at2; -.
DR   BioCyc; CORYNE:G18NG-10314-MONOMER; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000000582; Chromosome.
DR   AbasyAtlas; Q8NSC4; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071269; P:L-homocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0033353; P:L-methionine cycle; IEA:TreeGrafter.
DR   CDD; cd00401; SAHH; 1.
DR   FunFam; 3.40.50.720:FF:000004; Adenosylhomocysteinase; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR00936; ahcY; 1.
DR   NCBIfam; NF004005; PRK05476.2-3; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
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.
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..474
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116960"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         198..200
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         261..266
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         319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         340..342
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         388
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
SQ   SEQUENCE   474 AA;  51996 MW;  74673F92624C4F9D CRC64;
     MDFKVADLSL AEAGRHQIRL AEYEMPGLMQ LRKEFADEQP LKGARIAGSI HMTVQTAVLI
     ETLTALGAEV RWASCNIFST QDEAAAAIVV GSGTVEEPAG VPVFAWKGES LEEYWWCINQ
     IFSWGDELPN MILDDGGDAT MAVIRGREYE QAGLVPPAEA NDSDEYIAFL GMLREVLAAE
     PGKWGKIAEA VKGVTEETTT GVHRLYHFAE EGVLPFPAMN VNDAVTKSKF DNKYGTRHSL
     IDGINRATDM LMGGKNVLVC GYGDVGKGCA EAFDGQGARV KVTEADPINA LQALMDGYSV
     VTVDEAIEDA DIVITATGNK DIISFEQMLK MKDHALLGNI GHFDNEIDMH SLLHRDDVTR
     TTIKPQVDEF TFSTGRSIIV LSEGRLLNLG NATGHPSFVM SNSFADQTIA QIELFQNEGQ
     YENEVYRLPK VLDEKVARIH VEALGGQLTE LTKEQAEYIG VDVAGPFKPE HYRY
//