SAHH_DICDI
ID SAHH_DICDI Reviewed; 431 AA.
AC P10819; Q55F98;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=sahA; ORFNames=DDB_G0267418;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3288206; DOI=10.1016/s0006-291x(88)81231-2;
RA Kasir J., Aksamit R.R., Backlund P.S. Jr., Cantoni G.L.;
RT "Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from
RT Dictyostelium discoideum as deduced from the cDNA sequence.";
RL Biochem. Biophys. Res. Commun. 153:359-364(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-431.
RX PubMed=3139100; DOI=10.1016/0300-9084(88)90115-0;
RA Guitton M.C., Part D., Veron M.;
RT "Cloning of a cDNA for the S-adenosyl-L-homocysteine hydrolase from
RT Dictyostelium discoideum.";
RL Biochimie 70:835-840(1988).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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.
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;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31040.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M19937; AAA33165.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73161.1; -; Genomic_DNA.
DR EMBL; X12523; CAA31040.1; ALT_FRAME; mRNA.
DR PIR; A27655; A27655.
DR RefSeq; XP_647635.1; XM_642543.1.
DR AlphaFoldDB; P10819; -.
DR SMR; P10819; -.
DR STRING; 44689.DDB0191108; -.
DR PaxDb; P10819; -.
DR EnsemblProtists; EAL73161; EAL73161; DDB_G0267418.
DR GeneID; 8616450; -.
DR KEGG; ddi:DDB_G0267418; -.
DR dictyBase; DDB_G0267418; sahA.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; P10819; -.
DR OMA; NKYGCRE; -.
DR PhylomeDB; P10819; -.
DR Reactome; R-DDI-156581; Methylation.
DR Reactome; R-DDI-1614635; Sulfur amino acid metabolism.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:P10819; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031002; C:actin rod; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:dictyBase.
DR GO; GO:0030552; F:cAMP binding; TAS:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 3.
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 Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..431
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116911"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 222..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="E -> A (in Ref. 1; AAA33165)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Missing (in Ref. 1; AAA33165)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="N -> T (in Ref. 1; AAA33165)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="T -> H (in Ref. 1; AAA33165)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> G (in Ref. 3; CAA31040)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="D -> S (in Ref. 3; CAA31040)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..365
FT /note="FCNQT -> SVTK (in Ref. 3; CAA31040)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="F -> L (in Ref. 1; AAA33165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47280 MW; C621FC6BE5BCBA2A CRC64;
MTKLHYKVKD ISLAAWGRKE IEIAENEMPG LMTLRKKYGP AQILKGARIA GCLHMTIQTA
VLIETLTALG AQVQWSSCNI FSTQDQAAAA IAATGVPVYA WKGETEEEYN WCVEQTIVFQ
DGQPLNMILD DGGDLTNLVH EKYPQFLAGI KGISEETTTG VHNLYKMFKE GKLKVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ SLSKMGARVL
VTEIDPINAL QACMDGYQIV TMETAAPLSN IFVTTTGCRD IVRGEHFAVM KEDAIVCNIG
HFDCEIDVAW LNANAKKDTV KPQVDRYTLA NGVHIILLAE GRLVNLGCGT GHPSFVMSNS
FCNQTLAQIA LWTKTEEYPL GVHFLPKILD EEVARLHLDQ LGAKLTTLTE KQSEYLSVPV
AGPYKVDHYR Y
