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Database: UniProt
Entry: L0DEJ0_SINAD
LinkDB: L0DEJ0_SINAD
Original site: L0DEJ0_SINAD 
ID   L0DEJ0_SINAD            Unreviewed;       333 AA.
AC   L0DEJ0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Lactate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:AGA27076.1};
GN   OrderedLocusNames=Sinac_2783 {ECO:0000313|EMBL:AGA27076.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA27076.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA27076.1, ECO:0000313|Proteomes:UP000010798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC   {ECO:0000313|Proteomes:UP000010798};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP003364; AGA27076.1; -; Genomic_DNA.
DR   RefSeq; WP_015246227.1; NZ_JH621478.1.
DR   AlphaFoldDB; L0DEJ0; -.
DR   STRING; 886293.Sinac_2783; -.
DR   KEGG; saci:Sinac_2783; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_0; -.
DR   OrthoDB; 277029at2; -.
DR   Proteomes; UP000010798; Chromosome.
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; IPR029753; D-isomer_DH_CS.
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.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010798}.
FT   DOMAIN          4..328
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..297
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   333 AA;  36495 MW;  312E13C5E1FB83F1 CRC64;
     MKVAVFSTKP YDRSSLDGAN TEHGHELVYF DARLSAATAP LARGCEAVCA FVNDELNATV
     LEELHRSGVR FVALRCAGYN NVDHEVAERH RLVVARVPAY SPYAVAEHTV ALILSLNRKI
     YRAYNRVREG NFTLDGLLGF DLHGRTIGVI GTGQIGLEVA RIMRGFGCQV LAYDIKPNPE
     CESLQVRYVS LEDLLAKSDI ITLHCPLTPS TRHLIDTKSL QTMKPGVMII NTGRGSLVDT
     EAVIAGLKSA KIGYLGLDVY EEEADLFFED HSGQVIHDDV FARLLTFPNV LITGHQAFFT
     REALQGIATT TLANLTEFAE NGTCSNAVPS PKF
//
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