SAHH_PLACH
ID SAHH_PLACH Reviewed; 479 AA.
AC Q4XZZ5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN ORFNames=PC000295.02.0;
OS Plasmodium chabaudi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5825;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS;
RX PubMed=15637271; DOI=10.1126/science.1103717;
RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA Turner C.M.R., Waters A.P., Sinden R.S.;
RT "A comprehensive survey of the Plasmodium life cycle by genomic,
RT transcriptomic, and proteomic analyses.";
RL Science 307:82-86(2005).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; CAAJ01002012; CAH77515.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4XZZ5; -.
DR SMR; Q4XZZ5; -.
DR VEuPathDB; PlasmoDB:PCHAS_1236200; -.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; Q4XZZ5; -.
DR UniPathway; UPA00314; UER00076.
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 3: Inferred from homology;
KW Hydrolase; NAD; One-carbon metabolism.
FT CHAIN 1..479
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116916"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 263..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 342..344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 53671 MW; 7688F675C79422B6 CRC64;
MYDSTSKIKD LSLAPFGKLQ MEISETEMPG LMTIREEYEK LKPLKGAKIT GCLHMTIETA
LLMETLQKLG AKLRWCSCNI YSTLDYAAAA VSTLENVSVF AWRGETLEEY WWCVEKALTW
GENGEGPDLI VDDGADASYL VHKGAEYEKL YEEKKILPDP ETGKNEEERC FLSLIKSSIL
KNPKKWTNMS KKIIGMSEET TTGVLRVKKI EKNNGLLFTA INVNDSVTKQ KYDNIYGCRH
SLPDGLMRAT DFMISGKIVV ICGYGDVGKG CASAMKGLGA RVYVTEVDPI CAIQAVMEGF
NVVTLEEIVE KGDFFVTCTG NVDIIKLEHL LKMKNNAVVG NIGHFDDEIQ IADLFSHEGI
EIENVKPQVD RVTLPNGNKI IVLAQGRLLN LACATGHPAF VMSFSFCNQV FAQLELWENR
NTGKYEKNKS YILPKELDEK VAYYHLKKLN ATLTELDDNQ CEFLGVSKNG PFKSEAYRY
