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Database: UniProt
Entry: I0IB66_PHYMF
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Original site: I0IB66_PHYMF 
ID   I0IB66_PHYMF            Unreviewed;       518 AA.
AC   I0IB66;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN   Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563,
GN   ECO:0000313|EMBL:BAM02504.1};
GN   OrderedLocusNames=PSMK_03450 {ECO:0000313|EMBL:BAM02504.1};
OS   Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae; Phycisphaera.
OX   NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM02504.1, ECO:0000313|Proteomes:UP000007881};
RN   [1] {ECO:0000313|EMBL:BAM02504.1, ECO:0000313|Proteomes:UP000007881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC   {ECO:0000313|Proteomes:UP000007881};
RA   Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a key role in the regulation of the intracellular
CC       concentration of adenosylhomocysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_00563}.
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=3.13.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|PIRSR:PIRSR001109-2, 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|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|RuleBase:RU004166}.
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DR   EMBL; AP012338; BAM02504.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0IB66; -.
DR   STRING; 1142394.PSMK_03450; -.
DR   KEGG; phm:PSMK_03450; -.
DR   PATRIC; fig|1142394.8.peg.353; -.
DR   eggNOG; COG0499; Bacteria.
DR   HOGENOM; CLU_025194_2_1_0; -.
DR   OMA; YIGVTVE; -.
DR   OrthoDB; 9802717at2; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000007881; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00563}; Reference proteome {ECO:0000313|Proteomes:UP000007881}.
FT   DOMAIN          269..429
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         235..237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         298..303
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         300..305
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         321
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         356
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         377..379
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         423
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         430
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   518 AA;  56216 MW;  54B117837DE597A6 CRC64;
     MTAAPSVLNA PHDAPPGADP QHGDLPTAQT RGGLTFKVAD LSEESVRYGR TEIRLAEEEM
     PGLMACRREY GESQPLKGQR IMGSLHMTIQ TAVLIETLVE LGAEVRWVSC NIFSTQDHAA
     AAVVAGPSGT ADKPKGVPVY AWKGESLADY WWCTEQALRF ENGDGPTLIV DDGGDATMLI
     HKGVEFELAG SVPGPETTDN VEFKEVLKTL ARVQQETPDR WQKVAAACKG VSEETTTGIK
     ALNKLEKDGK LLFPAINVND SCTKSKFDNL YGCRHSLIDG LFRATDVMVS GKVAIVCGYG
     DVGKGCCQSL RGQGARVIVT EIDPICALQA AMEGYEVTTL EDALPEADIV ITTTGNYDII
     RLEHMQAMKD KTIVGNIGHF DNEIQMAKLE KAATRTNIKP QYDEWTFEDG HSILILAEGR
     LLNLGCATGH PSFVMSASFT NQTIAQIDLA LAANGQDSLS GLTYAENKVT LLPKILDEKV
     ARLHLGKLGV KLTELSEDQA DYIAVEKDGP YKPSHYRY
//
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