ID D1CFK4_THET1 Unreviewed; 413 AA.
AC D1CFK4;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563};
GN OrderedLocusNames=Tter_0793 {ECO:0000313|EMBL:ACZ41710.1};
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexota; Thermobaculum.
OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41710.1, ECO:0000313|Proteomes:UP000000323};
RN [1] {ECO:0000313|EMBL:ACZ41710.1, ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX PubMed=21304745;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL Stand. Genomic Sci. 3:153-162(2010).
RN [2] {ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine. {ECO:0000256|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=3.13.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|RuleBase:RU004166}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
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DR EMBL; CP001825; ACZ41710.1; -; Genomic_DNA.
DR AlphaFoldDB; D1CFK4; -.
DR STRING; 525904.Tter_0793; -.
DR KEGG; ttr:Tter_0793; -.
DR eggNOG; COG0499; Bacteria.
DR HOGENOM; CLU_025194_2_1_0; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000000323; Chromosome 1.
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; 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 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.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_00563}; Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT DOMAIN 180..341
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 146..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 209..214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 211..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 288..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 413 AA; 44836 MW; 4BC04D6EAD675826 CRC64;
MKDMSLAAKG HDRIAWAARE MPVLSRIADR FDREKPLAGV KIAACLHVTT ETANLMLTLM
RGGAEIALAA SNPLSTQDDV AAALVEKGIS VFAIKGEDED TYYSHIRAVL DTHPNITMDD
GADLVTTLHT ERLDIIDDVR AGTEETTTGV IRLKAMAADE QLKYPIIAVN EAYTKHLFDN
RYGTGQSTID GLLRATNILL AGKVFVVAGY GWCGKGLASR ARGMGCQVVV TEVDPIKALE
AVMDGFRVMP MTEAAKIADV IVTVTGGLHA VNAEAVQNLK DGVILANSGH FNDEIDIPAI
EKLSVARRMR RDFVEEFELK DGRKIYLLAE GRLLNLSAAE GHPAAVMDMS FANQALSIEW
LVNNASGLEP KVFSVPEEID RNVAQTKLES LGITIDKLSE EQLAYASEWR SGT
//
