SAHH_LUPLU
ID SAHH_LUPLU Reviewed; 485 AA.
AC Q9SP37;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=SAHH; Synonyms=SHH;
OS Lupinus luteus (European yellow lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3873;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RA Janowski R., Podkowinski J., Kisiel A., Jaskolski M.;
RT "S-adenosyl-L-homocysteinase cDNA sequence from Lupinus luteus.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC adenosyl-L-methionine-dependent methyl transferase reactions; therefore
CC adenosylhomocysteinase may play a key role in the control of
CC methylations via regulation of the intracellular concentration of
CC adenosylhomocysteine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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; AF185635; AAD56048.1; -; mRNA.
DR PDB; 3OND; X-ray; 1.17 A; A/B=1-485.
DR PDB; 3ONE; X-ray; 1.35 A; A/B=1-485.
DR PDB; 3ONF; X-ray; 2.00 A; A/B=1-485.
DR PDBsum; 3OND; -.
DR PDBsum; 3ONE; -.
DR PDBsum; 3ONF; -.
DR AlphaFoldDB; Q9SP37; -.
DR SMR; Q9SP37; -.
DR PRIDE; Q9SP37; -.
DR BRENDA; 3.3.1.1; 3093.
DR UniPathway; UPA00314; UER00076.
DR EvolutionaryTrace; Q9SP37; -.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; Hydrolase; NAD; One-carbon metabolism.
FT CHAIN 1..485
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116923"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 348..350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3ONF"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 142..160
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 406..425
FT /evidence="ECO:0007829|PDB:3OND"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:3OND"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:3OND"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:3OND"
SQ SEQUENCE 485 AA; 53326 MW; 42F8FA6C58A42B19 CRC64;
MALLVEKTTS GREYKVKDMS QADFGRLEIE LAEVEMPGLM ASRSEFGPSQ PFKGAKITGS
LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
TERALDWGPG GGPDLIVDDG GDTTLLIHEG VKAEEIYEKS GQFPDPDSTD NAEFKIVLSI
IKEGLKTDPK RYHKMKDRVV GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN
LYGCRHSLPD GLMRATDVMI AGKVAVVAGY GDVGKGCAAA LKQAGARVIV TEIDPICALQ
ATMEGLQVLT LEDVVSEADI FVTTTGNKDI IMLDHMKKMK NNAIVCNIGH FDNEIDMLGL
ETHPGVKRIT IKPQTDRWVF PETNTGIIIL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
LELWNEKSSG KYEKKVYVLP KHLDEKVAAL HLEKLGAKLT KLSKDQADYI SVPVEGPYKP
FHYRY
