ID W2ZAC3_PHYPR Unreviewed; 371 AA.
AC W2ZAC3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F442_09460 {ECO:0000313|EMBL:ETP43921.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP43921.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP43921.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP43921.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:ETP43921.1}.
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DR EMBL; ANIY01001986; ETP43921.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZAC3; -.
DR EnsemblProtists; ETP43921; ETP43921; F442_09460.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12183; LDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 44..370
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 153..339
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 371 AA; 40574 MW; F581080741197E2C CRC64;
MLAPRTVHPC TKILYFDLIA WVGHSSFCRE NRITTTNTMQ IAFFSSHSYD IESMERIAKE
QDITPKHELK FFTSRLDATS AKLAEGCEGV CIFVNDVADE AALRVLAAGG TKAMFLRCAG
FDMIDLKVAK ELGLAVTRVP AYSPYAVAEH AASLMMALNR KIHRSYNRTR EQNFRLAGLL
GFDINGKTIG VVGTGKIGAL FARIAAGFGA KVLGYDVVQN PEALSYGVEY VSLDEMWKRA
DIISLHCPLF PSTKHTINAD SISKMKKGVT IINTSRGGLI DNKALVDGLK SGKVGAVGLD
VFEGEGAYFY SDRSGVVIQD ETLARLFTFA NVLITGHQAF FTKEALDNIA LTTFANVKAY
EAKKTLVNEV K
//
