SAHH_BRAEL
ID SAHH_BRAEL Reviewed; 473 AA.
AC A0A087WNH6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 2.
DT 03-AUG-2022, entry version 37.
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=BeSAHase {ECO:0000303|PubMed:26627650};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000303|PubMed:26627650};
DE Short=SAHase {ECO:0000303|PubMed:26627650};
GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563};
OS Bradyrhizobium elkanii.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=29448;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH ADENOSINE AND NAD,
RP FUNCTION, COFACTOR, SUBUNIT, AND DOMAIN.
RC STRAIN=USDA 76 {ECO:0000305};
RX PubMed=26627650; DOI=10.1107/s1399004715018659;
RA Manszewski T., Singh K., Imiolczyk B., Jaskolski M.;
RT "An enzyme captured in two conformational states: crystal structure of S-
RT adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.";
RL Acta Crystallogr. D 71:2422-2432(2015).
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine, which is a strong inhibitor of
CC SAM-dependent methyltransferases. Catalyzes the hydrolysis of S-
CC adenosyl-L-homocysteine into L-homocysteine and adenosine.
CC {ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000305|PubMed:26627650}.
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 ECO:0000269|PubMed:26627650};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563,
CC ECO:0000269|PubMed:26627650};
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 -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:26627650}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- DOMAIN: Each protomer consists of two large domains, the substrate-
CC binding domain and the cofactor-binding domain, which are separated by
CC a deep crevice forming the substrate-access channel to the active site,
CC and a small C-terminal oligomerization domain.
CC {ECO:0000269|PubMed:26627650}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
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DR PDB; 4LVC; X-ray; 1.74 A; A/B/C/D=1-473.
DR PDB; 5M5K; X-ray; 1.84 A; A/B/C/D=1-473.
DR PDB; 5M65; X-ray; 1.95 A; A/B=1-473.
DR PDB; 5M66; X-ray; 1.95 A; A/B/C/D=1-473.
DR PDB; 5M67; X-ray; 1.54 A; A/B/C/D=1-473.
DR PDB; 6EXI; X-ray; 1.92 A; A/B/C/D=1-473.
DR PDBsum; 4LVC; -.
DR PDBsum; 5M5K; -.
DR PDBsum; 5M65; -.
DR PDBsum; 5M66; -.
DR PDBsum; 5M67; -.
DR PDBsum; 6EXI; -.
DR AlphaFoldDB; A0A087WNH6; -.
DR SMR; A0A087WNH6; -.
DR STRING; 398525.KB900701_gene6261; -.
DR eggNOG; COG0499; Bacteria.
DR BRENDA; 3.3.1.1; 9755.
DR UniPathway; UPA00314; UER00076.
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; 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; 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.
FT CHAIN 1..473
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000438794"
FT BINDING 58..62
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26627650"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000305|PubMed:26627650"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000305|PubMed:26627650"
FT BINDING 198..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|PubMed:26627650"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000305|PubMed:26627650"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000305|PubMed:26627650"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|PubMed:26627650"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:26627650"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|PubMed:26627650"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 340..342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|PubMed:26627650"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26627650"
FT BINDING 385
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|PubMed:26627650"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26627650"
FT BINDING 467
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:26627650"
FT BINDING 471
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:26627650"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5M65"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:5M67"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5M67"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5M67"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4LVC"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5M65"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 231..248
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:5M67"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 394..413
FT /evidence="ECO:0007829|PDB:5M67"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:5M67"
FT TURN 439..444
FT /evidence="ECO:0007829|PDB:5M67"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:5M67"
SQ SEQUENCE 473 AA; 52040 MW; 03435F6265F46D97 CRC64;
MNAKPGFTDY IVKDIALADF GRKEISLAET EMPGLMATRE EYGPKQPLKG ARIAGSLHMT
IQTAVLIETL AALGADIRWV SCNIYSTQDH AAAAIAAAGI PVFAVKGETL TEYWDYTAKL
FDWHGGGTPN MILDDGGDAT MLVHAGYRAE QGDTAFLDKP GSEEEEIFYA LVKRLLKEKP
KGWFAEIAKN IKGVSEETTT GVHRLYEMAN KGTLLFPAIN VNDSVTKSKF DNLYGCRESL
VDGIRRGTDV MLSGKVAMVA GFGDVGKGSA ASLRQAGCRV MVSEVDPICA LQAAMEGYEV
VTMEDAAPRA DIFVTATGNK DIITIEHMRA MKDRAIVCNI GHFDNEIQIA SLRNLKWTNI
KPQVDEIEFP DKHRIIMLSE GRLVNLGNAM GHPSFVMSAS FTNQTLAQIE LFANNKDSKY
AKKVYVLPKT LDEKVARLHL AKIGVKLTEL RKDQADYIGV KQEGPYKSDH YRY
