SAHH_THEMA
ID SAHH_THEMA Reviewed; 404 AA.
AC O51933;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 153.
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=TM_0172;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9440516; DOI=10.1128/jb.180.2.274-281.1998;
RA Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M.;
RT "Reverse gyrase from the hyperthermophilic bacterium Thermotoga maritima:
RT properties and gene structure.";
RL J. Bacteriol. 180:274-281(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AF013268; AAC01562.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35265.1; -; Genomic_DNA.
DR PIR; B72409; B72409.
DR RefSeq; NP_227987.1; NC_000853.1.
DR RefSeq; WP_004082805.1; NZ_CP011107.1.
DR PDB; 3X2E; X-ray; 2.85 A; A/B/C/D=2-404.
DR PDB; 3X2F; X-ray; 2.04 A; A/B=2-404.
DR PDB; 5TOV; X-ray; 1.90 A; A/B=1-404.
DR PDB; 5TOW; X-ray; 1.75 A; A/B=1-404.
DR PDBsum; 3X2E; -.
DR PDBsum; 3X2F; -.
DR PDBsum; 5TOV; -.
DR PDBsum; 5TOW; -.
DR AlphaFoldDB; O51933; -.
DR SMR; O51933; -.
DR STRING; 243274.THEMA_03940; -.
DR ChEMBL; CHEMBL1075032; -.
DR EnsemblBacteria; AAD35265; AAD35265; TM_0172.
DR KEGG; tma:TM0172; -.
DR eggNOG; COG0499; Bacteria.
DR InParanoid; O51933; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 522981at2; -.
DR BRENDA; 3.3.1.1; 6331.
DR SABIO-RK; O51933; -.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:O51933; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; NAD; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..404
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116995"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 140..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 203..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 282..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 329
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT CONFLICT 44
FT /note="A -> R (in Ref. 1; AAC01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="I -> V (in Ref. 1; AAC01562)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5TOV"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5TOW"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3X2F"
FT HELIX 338..358
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:5TOW"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:5TOW"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:5TOW"
SQ SEQUENCE 404 AA; 44850 MW; D20DB3BE02826148 CRC64;
MNTGEMKINW VSRYMPLLNK IAEEYSREKP LSGFTVGMSI HLEAKTAYLA ITLSKLGAKV
VITGSNPLST QDDVAEALRS KGITVYARRT HDESIYRENL MKVLDERPDF IIDDGGDLTV
ISHTEREEVL ENLKGVSEET TTGVRRLKAL EETGKLRVPV IAVNDSKMKY LFDNRYGTGQ
STWDAIMRNT NLLVAGKNVV VAGYGWCGRG IALRAAGLGA RVIVTEVDPV KAVEAIMDGF
TVMPMKEAVK IADFVITASG NTDVLSKEDI LSLKDGAVLA NAGHFNVEIP VRVLEEIAVE
KFEARPNVTG YTLENGKTVF LLAEGRLVNL AAGDGHPVEI MDLSFALQIF AVLYLLENHR
KMSPKVYMLP DEIDERVARM KLDSLGVKID ELTEKQRRYL RSWQ
