ID   SAHH_DROME              Reviewed;         432 AA.
AC   Q27580; Q8MZI1; Q9VXV5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN   Name=Ahcy13; Synonyms=ahcY; ORFNames=CG11654;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97188525; PubMed=9037110; DOI=10.1007/s004380050348;
RA   Caggese C., Ragone G., Barsanti P., Moschetti R., Messina A.,
RA   Massari S., Caizzi R.;
RT   "The S-adenosyl-L-homocysteine hydrolase of Drosophila melanogaster:
RT   identification, deduced amino acid sequence and cytological
RT   localization of the structural gene.";
RL   Mol. Gen. Genet. 253:492-498(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC       adenosyl-L-methinine-dependent methyl transferase reactions;
CC       therefore adenosylhomocysteinase may play a key role in the
CC       control of methylations via regulation of the intracellular
CC       concentration of adenosylhomocysteine.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine.
CC   -!- COFACTOR: Binds 1 NAD per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- INTERACTION:
CC       Q9VWD6:-; NbExp=1; IntAct=EBI-171029, EBI-161741;
CC       Q24106:W; NbExp=1; IntAct=EBI-171029, EBI-135509;
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
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DR   EMBL; X95636; CAA64892.1; -; mRNA.
DR   EMBL; AE014298; AAF48453.1; -; Genomic_DNA.
DR   EMBL; AY102668; AAM27497.1; -; mRNA.
DR   RefSeq; NP_511164.2; -.
DR   UniGene; Dm.7858; -.
DR   HSSP; P23526; 1LI4.
DR   SMR; Q27580; 3-432.
DR   IntAct; Q27580; 6.
DR   Ensembl; FBgn0014455; Drosophila melanogaster.
DR   GeneID; 32471; -.
DR   KEGG; dme:Dmel_CG11654; -.
DR   NMPDR; fig|7227.3.peg.17936; -.
DR   FlyBase; FBgn0014455; Ahcy13.
DR   HOGENOM; Q27580; -.
DR   OMA; Q27580; HMRAMKD.
DR   BRENDA; 3.3.1.1; 48.
DR   NextBio; 778633; -.
DR   ArrayExpress; Q27580; -.
DR   GermOnline; CG11654; Drosophila melanogaster.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000043; Ad_hcy_hydrolase.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   Gene3D; G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1.
DR   PANTHER; PTHR23420; Ad_hcy_hydrolase; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 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   Complete proteome; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN         1    432       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000116913.
FT   REGION      183    350       NAD binding (By similarity).
FT   BINDING      56     56       Substrate (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     156    156       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   CONFLICT    146    146       Y -> F (in Ref. 1; CAA64892).
FT   CONFLICT    265    265       A -> G (in Ref. 1; CAA64892).
FT   CONFLICT    294    294       A -> R (in Ref. 1; CAA64892).
FT   CONFLICT    326    328       DRY -> IRH (in Ref. 4; AAM27497).
FT   CONFLICT    331    331       Q -> K (in Ref. 1; CAA64892).
FT   CONFLICT    351    351       H -> D (in Ref. 1; CAA64892).
FT   CONFLICT    379    380       YA -> S (in Ref. 1; CAA64892).
SQ   SEQUENCE   432 AA;  47366 MW;  2977DAF12B40C324 CRC64;
     MSKPSYKVAD ISLAEWGRKA IIIAENEMPG LMACRKKYGP SKPLKGARIT GCLHMTVQTA
     VLIETLVELG AQVQWSSCNI FSTQDNAAAA IAATGVPVYA WKGETDEEYM WCIEQTLVFP
     DGQPLNMILD DGGDLTNLVH EKFPQYLKNI KGLSEETTTG VHNLYKMFKE GRLGVPAINV
     NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVCCVAG YGDVGKGCAQ ALKGFGGRVI
     VTEVDPINAL QAAMEGYEVT TMEEASKEAS IFVTTTGCRD IITSVHLQQM PDDAIVCNIG
     HFDIEIDVDW LNANAKEKVN VKPQVDRYTM QSGKHIILLA EGRLVNLGCA HGHPSFVMSN
     SFTNQVLAQI ELWTKSDKYA VGVHVLPKIL DEEVASLHLE KLGVKLTKLT EKQATYLGVS
     QTGPFKPDHY RY
//