(data stored in SCRATCH zone)

SWISSPROT: B6H9B6_PENRW

ID   B6H9B6_PENRW            Unreviewed;       448 AA.
AC   B6H9B6;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE            EC=3.3.1.1 {ECO:0000256|RuleBase:RU000548};
GN   ORFNames=Pc16g05080 {ECO:0000313|EMBL:CAP93178.1}, PCH_Pc16g05080
GN   {ECO:0000313|EMBL:CAP93178.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93178.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP93178.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-
CC         homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199;
CC         EC=3.3.1.1; Evidence={ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU000548};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|RuleBase:RU000548}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|RuleBase:RU004166}.
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DR   EMBL; AM920431; CAP93178.1; -; Genomic_DNA.
DR   RefSeq; XP_002560855.1; XM_002560809.1.
DR   STRING; 1108849.XP_002560855.1; -.
DR   EnsemblFungi; CAP93178; CAP93178; PCH_Pc16g05080.
DR   GeneID; 8306051; -.
DR   KEGG; pcs:Pc16g05080; -.
DR   eggNOG; KOG1370; Eukaryota.
DR   eggNOG; COG0499; LUCA.
DR   HOGENOM; HOG000227987; -.
DR   KO; K01251; -.
DR   OMA; QSTWDGI; -.
DR   OrthoDB; 371693at2759; -.
DR   BioCyc; PCHR:PC16G05080-MONOMER; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; IEA:InterPro.
DR   CDD; cd00401; SAHH; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR034373; Adenosylhomocysteinase.
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;
DR   PRODOM; B6H9B6.
DR   SWISS-2DPAGE; B6H9B6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000256|RuleBase:RU000548};
KW   NAD {ECO:0000256|RuleBase:RU000548};
KW   One-carbon metabolism {ECO:0000256|RuleBase:RU000548};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN      194    354       AdoHcyase_NAD. {ECO:0000259|SMART:
FT                                SM00997}.
FT   BINDING      58     58       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001109-1}.
FT   BINDING     134    134       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001109-1}.
FT   BINDING     159    159       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001109-1}.
FT   BINDING     189    189       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001109-1}.
FT   BINDING     193    193       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001109-1}.
SQ   SEQUENCE   448 AA;  48832 MW;  3BB0757E3469BF37 CRC64;
     MAAPAQKFKV ADLSLAAFGR REIELSEVEM PGLMAIREKY GADQPLKGAR IAGCLHMTIQ
     TAVLIETLTH LGAEVTWTSC NIFSTQDHAA AAIAAAGVPV FAWKGESEEE YQWCLDQQLQ
     AFKDGKKLNL ILDDGGDLTS LVHTKYPEML DDCFGVSEET TTGVHHLYKM MKENTLKVPA
     INVNDCVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALHSMGA
     RVIVTEVDPI NALQAAVQGY EVNTMEAAAP IGQIFVTTTG CRDILVGRHF EAMRNDAIVC
     NIGHFDIEID VAWLKANSQS VQNIKPQVDR YSLNGKNIIL LAEGRLVNLG CATGHSSFVM
     SCSFSNQVLA QIALFKAEDE AFGKKYIEFG AGGRKPVGVY VLPKQLDEQV ARCHLDHVNA
     KLTELTPVQA EYLSLPVNGP FKPEIYRY
//

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