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Database: UniProt
Entry: A0A0W0Z2Y9_9GAMM
LinkDB: A0A0W0Z2Y9_9GAMM
Original site: A0A0W0Z2Y9_9GAMM 
ID   A0A0W0Z2Y9_9GAMM        Unreviewed;       481 AA.
AC   A0A0W0Z2Y9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000313|EMBL:KTD63505.1};
GN   ORFNames=Lsha_0683 {ECO:0000313|EMBL:KTD63505.1};
OS   Legionella shakespearei DSM 23087.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD63505.1, ECO:0000313|Proteomes:UP000054600};
RN   [1] {ECO:0000313|EMBL:KTD63505.1, ECO:0000313|Proteomes:UP000054600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD63505.1,
RC   ECO:0000313|Proteomes:UP000054600};
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   -!- 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:KTD63505.1}.
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DR   EMBL; LNYW01000020; KTD63505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0Z2Y9; -.
DR   STRING; 1122169.Lsha_0683; -.
DR   PATRIC; fig|1122169.6.peg.780; -.
DR   eggNOG; COG0499; Bacteria.
DR   OrthoDB; 5637123at2; -.
DR   Proteomes; UP000054600; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KTD63505.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054600}.
FT   DOMAIN          238..309
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   481 AA;  53771 MW;  CF241B514D5B5716 CRC64;
     MLLMSNKYTK IGVLLVVYIT GVQLMQVFNK DELDKDADPI HFNGKVGYPD ISLPVLDSLL
     ERAYKEGKAN ILGKTAIFYV HHPLQTSINV VDALIHLGAK PKNLFILGKR YSECESVVST
     LVQKGVHYQP CSMQTALGQY SHSFIRDINW LWAKMVEKLD SQVEQILVMD HGGHAITYLP
     LALLEHYKVI GIEKTTAGFI NSERHGTPPI PVIDVANSAA KRFLESSLIA ETVVNKIDAY
     LPENINDFVF GVVGFGAIGK AVVNRLQQLG CRLIVHDIDS SQQHSIGKTK NIIFTNDMSA
     LVASADYIFG CSGRDISEGQ LEQLRLATRN KTLISCSSED KEYLSFLQMI NRQMPTVFDP
     MDDIEFKTEF GASVHLLRGG FPVNFDNTGE SVPANDIQLT RSLVVAAVLQ ASDYLNTTVL
     NGVYALDATY QRFVINEWLK HQDDPRIDRE NLTCFLDEDW LANHSNSAIS EFRGVLESER
     R
//
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