(data stored in SCRATCH zone)

SWISSPROT: D5EA49_METMS

ID   D5EA49_METMS            Unreviewed;       468 AA.
AC   D5EA49;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 72.
DE   RecName: Full=S-inosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            Short=SIHH {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.3.1.- {ECO:0000256|HAMAP-Rule:MF_00563};
GN   OrderedLocusNames=Mmah_0523 {ECO:0000313|EMBL:ADE36050.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36050.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36050.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of S-inosyl-L-homocysteine (SIH) to
CC       L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L-
CC       methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH)
CC       produced from SAM-dependent methylation reactions. Can also catalyze
CC       the reverse reaction in vitro, i.e. the synthesis of SIH from Hcy and
CC       inosine. {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-inosyl-L-homocysteine = inosine + L-homocysteine;
CC         Xref=Rhea:RHEA:59828, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596,
CC         ChEBI:CHEBI:57985, ChEBI:CHEBI:58199; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00563};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- MISCELLANEOUS: SAH is a product of SAM methyltransferases and is known
CC       to be a feedback inhibitor of these enzymes. As a result of this
CC       inhibition, organisms have evolved efficient enzymes to metabolize SAH
CC       via different pathways. The pathway found in methanogens differs from
CC       the canonical pathway, it uses the deamination of S-adenosyl-L-
CC       homocysteine to form S-inosyl-L-homocysteine for the regeneration of
CC       SAM from S-adenosyl-L-homocysteine. {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU004166}.
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DR   EMBL; CP001994; ADE36050.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADE36050; ADE36050; Mmah_0523.
DR   KEGG; mmh:Mmah_0523; -.
DR   eggNOG; arCOG04137; Archaea.
DR   eggNOG; COG0499; LUCA.
DR   HOGENOM; HOG000227986; -.
DR   KO; K01251; -.
DR   OMA; WTKPGEY; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; -; 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   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; D5EA49.
DR   SWISS-2DPAGE; D5EA49.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000313|EMBL:ADE36050.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00563};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          228..390
FT                   /note="AdoHcyase_NAD"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   NP_BIND         194..196
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   NP_BIND         257..262
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   NP_BIND         336..338
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         57
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         132
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         193
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         223
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         227
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         228
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         280
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         315
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         384
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
SQ   SEQUENCE   468 AA;  51780 MW;  4201974ACAC5E3CE CRC64;
     MVTNNDYKVK DIGLADSGRK QLNIAEQEMP GLMATREKYG PMKPLKGARI SGSLHMTVQT
     AVLIETLVEL GADVRWASCN IFSTQDEAAA AIADTGVPVF AWKGETLDDY WWCTKQALTW
     PDGKGPNLIV DDGGDATLMM HRGYAAEDDP SILDEPTDNK ELIAQNEVLK KSLKEDPQFW
     HKAVADWKGV SEETTTGVHR LYHWERKGEL LTPAINVNDS VTKSKFDNVY GCRESLVDAI
     KRGTDVMIAG KVAVVCGYGD VGKGSAAALA NHKARVIITE TDPICALQAL MEGYDVMTVE
     DALPYGDIYV TTTGNCDVLT TEHMSNMKDQ AIVCNIGHFD NEIQVDALNK MDNVKKVNIK
     PQVDEYQFPD GHSIYVLAEG RLVNLGLATG HPSFVMSNSF TNQTLAQIDL WESPKEVGVY
     RLSKVLDEEV ARLHLEKLGA KLTKMSQEQA EYIGFPVEGP YKPEHYRY
//

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