ID A0A0W0TTS3_9GAMM Unreviewed; 282 AA.
AC A0A0W0TTS3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000313|EMBL:KTC98837.1};
DE EC=3.3.1.1 {ECO:0000313|EMBL:KTC98837.1};
DE Flags: Fragment;
GN Name=sahH_1 {ECO:0000313|EMBL:KTC98837.1};
GN ORFNames=Lgee_1414 {ECO:0000313|EMBL:KTC98837.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC98837.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTC98837.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC98837.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTC98837.1}.
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DR EMBL; LNYC01000055; KTC98837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0TTS3; -.
DR STRING; 45065.Lgee_1414; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KTC98837.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000054785}.
FT DOMAIN 200..282
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT NON_TER 282
FT /evidence="ECO:0000313|EMBL:KTC98837.1"
SQ SEQUENCE 282 AA; 30902 MW; 5A3BE8EAF25C1D5B CRC64;
MEQRILEKVV SSGDYRVKDM SLAAWGRREI AIAETEMPGL MALRKEYGLQ KPLQGARIAG
CLHMTIQTAV LIETLTALGA EVRWSSCNIF STQDHAAAAI AATGVPVFAW KGETEEEYWW
CVEQTLKGPD GWSPNMILDD GGDLTLVVHE KYPHLLEEIR GISEETTTGV ARLYDMARKG
ELKVPAINVN DSVTKSKFDN LYGCRESLLD GLKRATDVMI AGKTALILGY GDVGKGCAQA
LRGQGAQVWI SEIDPICALQ AAMEGYRVVR LDEVAEDVDI LV
//
