GenomeNet

Database: UniProt
Entry: S4RRG8_PETMA
LinkDB: S4RRG8_PETMA
Original site: S4RRG8_PETMA 
ID   S4RRG8_PETMA            Unreviewed;       433 AA.
AC   S4RRG8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Adenosylhomocysteinase {ECO:0000313|Ensembl:ENSPMAP00000007804.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000007804.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000007804.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00036565};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC         Evidence={ECO:0000256|ARBA:ARBA00036565};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001109-2};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2};
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   Ensembl; ENSPMAT00000007839.1; ENSPMAP00000007804.1; ENSPMAG00000007048.1.
DR   GeneTree; ENSGT00950000182981; -.
DR   HOGENOM; CLU_025194_2_1_1; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
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   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245300}.
FT   DOMAIN          192..353
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         158..160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         223..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         300..302
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         354
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   433 AA;  48074 MW;  7D361FDC006C3B91 CRC64;
     VDRPSPPLTA DISLAEWGRK ALDIAENEMP GLMKMRQMYG KSKPLTGARI SGCLHMTVQT
     AVLIETLVEL GLQVMWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY VWCIEQTLIF
     PDGKPLNMIL DDGGDLTNLV HTKHPELLKG IRGVSEETTT GVHNLYKMLK NNELKIPAIN
     VNDSVTKSKF DNLYGCRESL IDGIKRATDV MIAGKVAVVA GYGDVGKGSA QSLRSFGARV
     IITEIDPINA LQAAMEGYEV TTMDEACKEA NIFVTTTGCK DIITGRHFEQ MKEDSIVCNI
     GHFDCELDVK WLNDHAAEKI NIKPQVDRYR LKNGRHVILL AEGRLVNLGC AMGHPSFVMS
     NSFTNQVLAQ IELWKHTDKY PLGVHFLPKK SDNASIRVRI STPTARDTFF TQKQXSYLSI
     PREGPLKPDH YRY
//
DBGET integrated database retrieval system