ID A0A3Q0FPJ3_ALLSI Unreviewed; 515 AA.
AC A0A3Q0FPJ3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN Name=AHCYL1 {ECO:0000313|RefSeq:XP_025049202.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025049202.1};
RN [1] {ECO:0000313|RefSeq:XP_025049202.1}
RP IDENTIFICATION.
RG RefSeq;
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|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2,
CC 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|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR RefSeq; XP_025049202.1; XM_025193417.1.
DR AlphaFoldDB; A0A3Q0FPJ3; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:RHEA.
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 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:SF3; S-ADENOSYLHOMOCYSTEINE HYDROLASE-LIKE PROTEIN 1; 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 Hydrolase {ECO:0000256|RuleBase:RU000548,
KW ECO:0000313|RefSeq:XP_025049202.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000548};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 274..435
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 37..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 305..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 429
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 515 AA; 57512 MW; BC1F3CC2840CDFF3 CRC64;
MKQAKEIEDA EKFNFMATVT KAPKKIQFAD DMQEFTKFPT KSGRRSLSRS ISQSSTDSYS
SAASYTDSSD DEEGTPREKH QTNSKGSSNF CVKNIKQAEF GRREIEIAEQ DMSALISLRK
RAQGEKPLAG AKIVGCTHIT AQTAVLIETL CALGAQCRWS ACNIYSTQNE VAAALAEAGV
AVFSWKGESE DDFWWCIDRC VNMDGWQPNM ILDDGGDLTH WVYKKYPNVF KKIRGIVEES
VTGVHRLYQL SKAGKLCVPA MNVNDSVTKQ KFDNLYCCRE SILDGLKRTT DVMFGGKQVV
VCGYGEVGKG CCAALKALGA IVYITEIDPI CALQACMDGF RVVKLNEVIR QMDVVITCTG
NKNVVTREHL DRMKNSCIVC NMGHSNTEID VTSLRTPELT WERVRSQVDH IIWPDGKRVV
LLAEGRLLNL SCSTVPTFVL SITATTQALA LIELYNAPEG RYKQDVYLLP KKMDEYVASL
HLPSFDAHLT ELTDDQAKYM GLNKNGPFKP NYYRY
//
