ID D1B5H6_THEAS Unreviewed; 411 AA.
AC D1B5H6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN OrderedLocusNames=Taci_1035 {ECO:0000313|EMBL:ACZ19267.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19267.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ19267.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
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|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2,
CC 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|RuleBase:RU000548}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001818; ACZ19267.1; -; Genomic_DNA.
DR RefSeq; YP_003317549.1; NC_013522.1.
DR AlphaFoldDB; D1B5H6; -.
DR STRING; 525903.Taci_1035; -.
DR EnsemblBacteria; ACZ19267; ACZ19267; Taci_1035.
DR KEGG; tai:Taci_1035; -.
DR PATRIC; fig|525903.6.peg.1033; -.
DR eggNOG; COG0499; Bacteria.
DR HOGENOM; CLU_025194_0_2_0; -.
DR OrthoDB; 9802717at2; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000002030; Chromosome.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:RHEA.
DR GO; GO:0006730; P:one-carbon metabolic process; 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 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; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:ACZ19267.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000548};
KW Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT DOMAIN 182..343
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 148..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 213..218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 290..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 411 AA; 45540 MW; 6FD076EA3B3DED16 CRC64;
MTLKDHELLA SGERKISWAW RYMPVLKELK ARHQAERPLE GRKLACCLHL EAKTACLLLA
LKDLGAQVFA AGSNPLSTQD DVCAALRERG VTVHSRRGMT ADEYVENLRR CLMEGPDFII
DDGADMVYVL HSEMPHLLKD LKGGCEETTT GIKRLKAMHR EGFLKIPMIA VNDALSKYLF
DNRYGTGQSV WDAISRLTNR IVAGSTVVVV GYGWCGKGVA RRAQGLGARV VVTEVDPHKA
LEAHMDGFSV MPLLEAAKVG DFFITVTGNT RVIRSEHFSV MKDGAILANA GHFDVEVCIP
DLEALSRSVE ESRPNVRSYR MEDGRELHLL AEGRLVNLAG GDGHPVEIMD LSFSSQLLSA
LFLVDNPMAP GVYPMPLQLD EEIARLKLSS LGIAIDRLTE EQRLYLESFR E
//
