ID   A0A3B3ZLD9_9GOBI        Unreviewed;       559 AA.
AC   A0A3B3ZLD9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000005226.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000005226.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122}.
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DR   AlphaFoldDB; A0A3B3ZLD9; -.
DR   STRING; 409849.ENSPMGP00000005226; -.
DR   Ensembl; ENSPMGT00000005544.1; ENSPMGP00000005226.1; ENSPMGG00000004357.1.
DR   Proteomes; UP000261520; 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   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; 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   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};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT   DOMAIN          310..471
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62162 MW;  6EB3ABED37246C93 CRC64;
     MSELATGEAK AEGKQASKEV KESENVAEKY SAMTVSKNSE MNMGDLTTVL SAVPTHKPVK
     KQIQFVEDKQ EFSRFPTKTG RRSLSRSISQ SSTDSYSSAA SYTDSSDDET SPRDKTQVNV
     KGSSDFCVKN IKQAEFGRRE IEIAEQDMAA LISLRKRAQS EKPLAGAKIV GCTHITAQTA
     VLIETLVALG AQCRWTACNI YSTQNEVAAA LAESGVAVFA WKGESEDDFW WCIDCCVNTE
     GWQPNMILDD GGDLTHWMYK KYPNVFKKIR GIVEESVTGV HRLYQLSKAG KLCVPAMNVN
     DSVTKQKFDN LYCCRESILD GLKRTTDVMF GGKQVVVCGY GEVGKGCCAA LKALGAIVYV
     TEIDPICALQ ACMDGFRVVK LNEIIRHVDV IITCTGNKNV VTRDQLDRMK NGSIVCNMGH
     SNTEIDVASL RTPELTWERV RSQVDHVIWP DGKRVILLAE GRLLNLSCST VPTFVLSITA
     TTQVSKIIAL HTEFEHVIIK IFYKLLKYEY VASLHLATFD AHLTELSDEQ AKYLGLNKNG
     PFKPNYYRYR HSNDSSYEM
//