ID C1LDH9_SCHJA Unreviewed; 456 AA.
AC C1LDH9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Putative adenosylhomocysteinase 3 {ECO:0000313|EMBL:CAX72757.1};
DE EC=3.3.1.1 {ECO:0000313|EMBL:CAX72757.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:CAX72757.1};
RN [1] {ECO:0000313|EMBL:CAX72757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72757.1};
RX DOI=10.1038/nature08140;
RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT "The Schistosoma japonicum genome reveals features of host-parasite
RT interplay.";
RL Nature 460:345-351(2009).
RN [2] {ECO:0000313|EMBL:CAX72757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72757.1};
RA Gang L.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN317026; CAX72757.1; -; mRNA.
DR AlphaFoldDB; C1LDH9; -.
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; 1.
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:SF0; ADENOSYLHOMOCYSTEINASE; 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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000313|EMBL:CAX72757.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT DOMAIN 288..449
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50754 MW; 55671497E0D0379F CRC64;
MSRLQQTNAD KMHEISSITL HSRDNSSYEE QVKIFSQDSR RMSTSAKKRL PSRSNSETGS
YDSASYSGSS SDDDDDESQQ RENPKERYLK PGLRAVNSRG FNDFCVQKIS QASFGRREIE
IAEQEMPGLM ALRKRAKTDQ PLKGAKILGC THVTAHTAVL IETMVCLGAQ VRWCACNIYS
TQNEVAAALA ESGLAIYAWK GETEEDFWWC IDRCICAEGW SPNVVLDDGG DLTHRLHKNY
KELLSGICGI VEESVTGVHR LYQYVKSGTL SVPAMNISDS ITKSKFDNFY LCKESIVDSL
KRTTDMMISG KTVLVCGYGE VGKGVCQALR GLGAFVCISE IDPICALQAC MDGYRVVKIE
EVIRTVDIVA TCTGNKDVIT RAHMDQMKNG CVVCNMGHSN TEIDVRSLQT PDLTWERVRS
QVDHIIWMDG KRIVLIAEGR LANLSCSTVS IYCRFC
//
