ID A0A158NRY3_ATTCE Unreviewed; 443 AA.
AC A0A158NRY3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN Name=105623507 {ECO:0000313|EnsemblMetazoa:XP_012060291.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012060291.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012060291.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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 EMBL; ADTU01024300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012060291.1; XM_012204901.1.
DR AlphaFoldDB; A0A158NRY3; -.
DR STRING; 12957.A0A158NRY3; -.
DR EnsemblMetazoa; XM_012204901.1; XP_012060291.1; LOC105623507.
DR GeneID; 105623507; -.
DR KEGG; acep:105623507; -.
DR eggNOG; KOG1370; Eukaryota.
DR InParanoid; A0A158NRY3; -.
DR OrthoDB; 120477at2759; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000005205; Unassembled WGS sequence.
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; 2.
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: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 Hydrolase {ECO:0000256|RuleBase:RU000548};
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:UP000005205}.
FT DOMAIN 163..324
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 194..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 443 AA; 49294 MW; 8E94409DFF303BAB CRC64;
MPGIMALRKR AGDDKPLKNA KIVGCTHINA QTAVLIETLV ELGAQVRWAA CNIYSTQNEV
AAALAYAGYP VFAWRGETEE DFWWCIDKCV AAENWQPNMI LDDGGDATHL MLKKYNAMFK
MIQGIVEESV TGVHRLYQLS KAGKLSVPAM NVNDSVTKTK FDNLYSCRES IIDSLKRSTD
IMFGGKQVVI CGYGEVGKGC CQALKGLGCI VYITEIDPIC ALQASMDGFR VMKLNEVIRN
VDIVITATGN KNVVTREHMD KMKNGCVVCN MGHSNTEIDV NSLRTPDLTW EKVRSQVDHV
IWPDGKRIVL LAEGRLVNLS CSSIPSFVVS ITAATQALAL IELFNAPPGR YKSDVYLLPK
KMDEYVASLH LPTFDAHLTE LTDEQAKYMG LNKAGPFKPN YYRLLSLKSC QIVHANKPTH
KKSLVEYCCR YKCESCIVCK PKR
//
