ID Q1LJ11_CUPMC Unreviewed; 327 AA.
AC Q1LJ11;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Phosphonate dehydrogenase (NAD-dependent phosphite dehydrogenase) {ECO:0000313|EMBL:ABF09865.1};
DE EC=1.20.1.1 {ECO:0000313|EMBL:ABF09865.1};
GN Name=ptxD {ECO:0000313|EMBL:ABF09865.1};
GN OrderedLocusNames=Rmet_2992 {ECO:0000313|EMBL:ABF09865.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF09865.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000352; ABF09865.1; -; Genomic_DNA.
DR RefSeq; WP_011517523.1; NC_007973.1.
DR AlphaFoldDB; Q1LJ11; -.
DR SMR; Q1LJ11; -.
DR STRING; 266264.Rmet_2992; -.
DR GeneID; 83661967; -.
DR KEGG; rme:Rmet_2992; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_4; -.
DR Proteomes; UP000002429; 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 GO; GO:0050609; F:phosphonate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:ABF09865.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT DOMAIN 6..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 327 AA; 35162 MW; 4441D2859C0E6D18 CRC64;
MNHRKIVVTQ PVHEEVLRKL QAEGEVIMNP GPDPWSPSQL REYLVDADAM MAFMTDSVTK
ESLLNAPRLK TISCALKGYD NFDLRACAQA GVSVTFVPDL LTEPTAELAI GLAIAAGRNV
LQGDAATRAG YSGWRPALYG TGLHGSVASV IGLGKVGQAI LARLAGFGCA RLLGVDPSVR
LDQVELVTLD EAVSTSDYVF LAVPLVSDTR HLVDSRMLQL SKKGQILVNV GRGSVVDERA
VVDALANEQL GAYAADVYEM EDWLLPDRPR EIHPGLTNNA RTVLTPHIGS AVRRVRFEIE
MRAAENLVRS LRGESLSDVA VEASAAA
//
