ID A0A0J5QDE1_9RHOB Unreviewed; 322 AA.
AC A0A0J5QDE1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lactate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:KMK65489.1};
GN ORFNames=IMCC21224_11320 {ECO:0000313|EMBL:KMK65489.1};
OS Puniceibacterium sp. IMCC21224.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK65489.1, ECO:0000313|Proteomes:UP000036046};
RN [1] {ECO:0000313|EMBL:KMK65489.1, ECO:0000313|Proteomes:UP000036046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK65489.1,
RC ECO:0000313|Proteomes:UP000036046};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21224 belonging to the
RT Alphaproteobacteria.";
RL Submitted (MAY-2015) 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}.
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:KMK65489.1}.
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DR EMBL; LDPY01000001; KMK65489.1; -; Genomic_DNA.
DR RefSeq; WP_047993849.1; NZ_LDPY01000001.1.
DR AlphaFoldDB; A0A0J5QDE1; -.
DR STRING; 1618204.IMCC21224_11320; -.
DR PATRIC; fig|1618204.4.peg.331; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000036046; 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; cd05301; GDH; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000036046}.
FT DOMAIN 6..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 34092 MW; A38296C0D4CCD366 CRC64;
MTKKKVLLTR RWPQSVEARL SETYDTTLNT QDIPMSPEAI GIALNEFDAV CPTVSDKLPA
SIFSGGQRAQ ILGNYGVGFN HIDIAAATGA GLTVTNTPGV LTDCTADTAL TLLLMLARRA
GEGERELRAG KWTGWRPTHM MGMRLSGKVL GIIGMGRIGI ATARRAQAAF GMKVVYFNRS
TPSDSDLSGL DAQRLETVED VLKAADVVSL HIPGGGANTH MMNSERLALI GPEGLLINSA
RGDIIDQTAL IAALKNGTIG GAGLDVFEGE PDVPAELIAM ENTVLLPHLG SATRETREEM
GNMVADNLDA FFAGQPVPNP VS
//
