ID T1PCH0_MUSDO Unreviewed; 432 AA.
AC T1PCH0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN Name=101893702 {ECO:0000313|EnsemblMetazoa:MDOA007568-PA};
GN Synonyms=LOC101893702 {ECO:0000313|RefSeq:XP_005184146.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP60459.1};
RN [1] {ECO:0000313|EMBL:AFP60459.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALHF {ECO:0000313|EMBL:AFP60459.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AFP60459.1};
RA Liu N., Zhang L., Li M., Reid W.;
RT "Transcriptome of adult Musca domestica launches a platform for comparative
RT house fly gene expression and characterization of differential gene
RT expression among resistant and susceptible house flies.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:MDOA007568-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA007568-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_005184146.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005184146.1};
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 EMBL; KA645830; AFP60459.1; -; mRNA.
DR RefSeq; XP_005184146.1; XM_005184089.3.
DR STRING; 7370.T1PCH0; -.
DR EnsemblMetazoa; MDOA007568-RA; MDOA007568-PA; MDOA007568.
DR GeneID; 101893702; -.
DR KEGG; mde:101893702; -.
DR VEuPathDB; VectorBase:MDOA007568; -.
DR eggNOG; KOG1370; Eukaryota.
DR OrthoDB; 120477at2759; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:AFP60459.1};
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:UP000694905}.
FT DOMAIN 191..352
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 157..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 222..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 432 AA; 47417 MW; F947D882A6A3637C CRC64;
MSKPTYKVAD IKLAEWGRKA IIIAENEMPG LMACRKKYGP SKILKGARIA GCLHMTVQTA
VLIETLVELG AEVQWSSCNI FSTQDHAAAA IAATGVPVYA WKGETEEEYQ WCIEQTLVFP
DGQPLNMILD DGGDLTNLVH EKYPQYLKGI KGLSEETTTG VHNLYKMFKE GRLGVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVCVVAG YGDVGKGCAQ ALKGFGGRVL
ITEIDPINAL QAAMEGYEVT TMEEASKEAT IFVTTTGCID IITGEHFLNM NDDAVVCNIG
HFDCEIDVAW LNTNAVEKVN VKPQVDRYTL PNGRHIIVLA EGRLVNLGCA HGHPSFVMSN
SFTNQVLAQI ELWTKSEQYA VGVHVLPKHL DEEVASLHLE KLGVKLTKLS EKQAKYLGIP
INGPFKPDHY RY
//
