ID A0A0V0WTF2_9BILA Unreviewed; 575 AA.
AC A0A0V0WTF2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Putative adenosylhomocysteinase 3 {ECO:0000313|EMBL:KRX79055.1};
GN Name=AHCYL2 {ECO:0000313|EMBL:KRX79055.1};
GN ORFNames=T06_7703 {ECO:0000313|EMBL:KRX79055.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79055.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79055.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79055.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX79055.1}.
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DR EMBL; JYDK01000058; KRX79055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WTF2; -.
DR STRING; 92179.A0A0V0WTF2; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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: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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 334..495
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 56..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63091 MW; 1057EA3847FB926E CRC64;
MMTSKKSENG EYQAETAPCC TAGCWNHRHH QHNSSHCDRY AARKPSIQFD RSSLLTTATN
GNGSDNGNGG GGGGGKICKP TSSLSTSTST TTTTTTSGSA ATHVVPTIIV DDVSKKTPST
IPCDSESDED QQEASPRISV KRTDSGFEDF CVRNLTIAKY GRKEIEIAEQ EMPGMMTLLE
RVGAEKPLKN AQIVGCTHIT AQTGVLIRTL IQLGASVRWC ACNIYSTQDE VAAALANENI
PIFAWEGETE EEFWWCIDKC VSAGHWRPNL IVDDGGDMTS YVAKTYPTVF AQLKGIVEES
LHGVHRLYNM SKTEQLAAPA MNINDSVLKA RFDSVYSCRE SIIDCLKRTT DSMLGGKQAV
ICGYGDIGKG VSNALKGLGV NVVVTEIDPI CALQACMEGF RVVRLEDVAQ QVDIVITCTS
NQHVVTRNLM NQMKSGCILC NMGRSNTVID VPSLRTKDLT WERLRLQVDH IIWPNGKRLV
LLAQGRQVCP SCSCVPSLVI SITATTQILA LIELFTSQRG RYKKDVYLMP KKMDEYVASL
HLPFFGANLT ELTDAQAEYL GVNKTGPFKQ NYYRY
//
