SAHH3_PONAB
ID SAHH3_PONAB Reviewed; 508 AA.
AC Q5R889;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Putative adenosylhomocysteinase 3;
DE Short=AdoHcyase 3;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase 3;
DE AltName: Full=S-adenosylhomocysteine hydrolase-like protein 2;
GN Name=AHCYL2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May regulate the electrogenic sodium/bicarbonate
CC cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary
CC of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol
CC 1,4,5-trisphosphate. {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000250|UniProtKB:Q96HN2}.
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=3.3.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer. Forms heteromultimers with AHCYL1 (via the C-
CC terminal region). Interacts with ITPR1; with lower affinity than AHCYL1
CC and maybe via ITPR1. Interacts with SLC4A4. Interacts with ZCCHC4 (By
CC similarity). {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000250|UniProtKB:Q96HN2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000250|UniProtKB:Q68FL4}. Microsome
CC {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with membranes when
CC phosphorylated, probably through interaction with ITPR1.
CC {ECO:0000250|UniProtKB:Q68FL4}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; CR859865; CAH92021.1; -; mRNA.
DR RefSeq; NP_001126174.1; NM_001132702.1.
DR AlphaFoldDB; Q5R889; -.
DR SMR; Q5R889; -.
DR STRING; 9601.ENSPPYP00000020187; -.
DR GeneID; 100173136; -.
DR KEGG; pon:100173136; -.
DR CTD; 23382; -.
DR eggNOG; KOG1370; Eukaryota.
DR InParanoid; Q5R889; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 3.
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 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Microsome; NAD;
KW One-carbon metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..508
FT /note="Putative adenosylhomocysteinase 3"
FT /id="PRO_0000230302"
FT REGION 24..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 298..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 354
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 375..377
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
SQ SEQUENCE 508 AA; 56679 MW; A59869443CC8F707 CRC64;
MLGSKKKYIV NGNSGIKAQI QFADQKQEFN KRPTKIGRRS LSRSISQSST DSYSSAASYT
DSSDDETSPR DKQQKNSKGS SDFCVKNIKQ AEFGRREIEI AEQEMPALMA LRKRAQGEKP
LAGAKIVGCT HITAQTAVLM ETLGALGAQC RWAACNIYST LNEVAAALAE SGFPVFAWKG
ESEDDFWWCI DRCVNVEGWQ PNMILDDGGD LTHWIYKKYP NMFKKIKGIV EESVTGVHRL
YQLSKAGKLC VPAMNVNDSV TKQKFDNLYC CRESILDGLK RTTDMMFGGK QVVVCGYGEV
GKGCCAALKA MGSIVYVTEI DPICALQACM DGFRLVKLNE VIRQVDIVIT CTGNKNVVTR
EHLDRMKNSC IVCNIGHSNT EIDVASLRTP ELTWERVRSQ VDHVIWPDGK RIVLLAEGRL
LNLSCSTVPT FVLSITATTQ ALALIELYNA PEGRYKQDVY LLPKKMDEYV ASLHLPTFDA
HLTELTDEQA KYLGLNKNGP FKPNYYRY
