SAHH_ANOGA
ID SAHH_ANOGA Reviewed; 432 AA.
AC O76757; Q7QEC2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=Ahcy13; ORFNames=AGAP000719;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=G3;
RA Zhao Y., Lu W., Eggleston P.;
RT "The S-adenosyl-L-homocysteine hydrolase of Anopheles gambiae.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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}.
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DR EMBL; AF080546; AAC29475.1; -; mRNA.
DR EMBL; AAAB01008847; EAA06909.2; -; Genomic_DNA.
DR RefSeq; XP_311257.2; XM_311257.4.
DR AlphaFoldDB; O76757; -.
DR SMR; O76757; -.
DR STRING; 7165.AGAP000719-PA; -.
DR PaxDb; O76757; -.
DR GeneID; 1272312; -.
DR KEGG; aga:AgaP_AGAP000719; -.
DR CTD; 1272312; -.
DR VEuPathDB; VectorBase:AGAP000719; -.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; O76757; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; O76757; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000007062; Chromosome X.
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-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; 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 2: Evidence at transcript level;
KW Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..432
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116912"
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 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="K -> R (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> V (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Y -> K (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="E -> D (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> P (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="A -> V (in Ref. 1; AAC29475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47680 MW; 6B384DCE94DDA1D3 CRC64;
MAKPAYKVAD ISLAEFGRKE IVLAENEMPG LMACRQKYGP LKILKGARIA GCLHMTIQTA
VLIETLIELG AEVQWSSCNI FSTQDHAAAA MAKAGVPVYA WKGETDEEYM WCIRQTLIFP
DGKPLNMILD DGGDLTNLVH AEHPELLKEI RGLSEETTTG VHNLYKMFRE GRLGMPAINV
NDSVTKSKFD NLYGCRESLL DGIKRATDVM IAGKVCVVAG YGDVGKGCAQ ALRGSGGRVL
ITEIDPINAL QAAMEGYEVT TMEEASKEAQ IFVTTTGCTD IIMGEHFLNM KDDSIVCNIG
HFDCEINVTW LQENAVEKVN IKPQVDRYRL ANGNHIILLA EGRLVNLGCA MGHSSFVMSN
SFTNQVLAQI ELWTNREQYA IGVHVLPKKL DEEVAALHLD KLGVKLTKLS ARQAEYLNLP
AEGPYKPEHY RY
