PTXD_PSEST
ID PTXD_PSEST Reviewed; 336 AA.
AC O69054;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphonate dehydrogenase;
DE EC=1.20.1.1;
DE AltName: Full=NAD-dependent phosphite dehydrogenase;
GN Name=ptxD;
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WM88;
RX PubMed=9791102; DOI=10.1128/jb.180.21.5547-5558.1998;
RA Metcalf W.W., Wolfe R.S.;
RT "Molecular genetic analysis of phosphite and hypophosphite oxidation by
RT Pseudomonas stutzeri WM88.";
RL J. Bacteriol. 180:5547-5558(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=WM88;
RX PubMed=11278981; DOI=10.1074/jbc.m011764200;
RA Costas A.M.G., White A.K., Metcalf W.W.;
RT "Purification and characterization of a novel phosphorus-oxidizing enzyme
RT from Pseudomonas stutzeri WM88.";
RL J. Biol. Chem. 276:17429-17436(2001).
CC -!- FUNCTION: Catalyzes phosphite (phosphonate) oxidation.
CC {ECO:0000269|PubMed:11278981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + phosphonate = H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:13173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16215, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.20.1.1;
CC Evidence={ECO:0000269|PubMed:11278981};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl, NADH and sulfite.
CC {ECO:0000269|PubMed:11278981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.25-7.75.;
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11278981}.
CC -!- INDUCTION: By phosphate starvation. {ECO:0000269|PubMed:11278981}.
CC -!- MASS SPECTROMETRY: Mass=36413; Mass_error=18; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11278981};
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF061070; AAC71709.1; -; Genomic_DNA.
DR RefSeq; WP_003118429.1; NZ_RHQY01000096.1.
DR PDB; 4E5K; X-ray; 1.95 A; A/B/C/D=1-329.
DR PDB; 4E5M; X-ray; 1.85 A; A/B=1-329.
DR PDB; 4E5N; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-330.
DR PDB; 4E5P; X-ray; 1.90 A; A/B/C/D/E/F=1-331.
DR PDB; 4EBF; X-ray; 2.30 A; A/B/C/D/E/F=1-331.
DR PDB; 4NU5; X-ray; 2.35 A; A/B=1-329.
DR PDB; 4NU6; X-ray; 2.65 A; A/B=1-329.
DR PDBsum; 4E5K; -.
DR PDBsum; 4E5M; -.
DR PDBsum; 4E5N; -.
DR PDBsum; 4E5P; -.
DR PDBsum; 4EBF; -.
DR PDBsum; 4NU5; -.
DR PDBsum; 4NU6; -.
DR AlphaFoldDB; O69054; -.
DR SMR; O69054; -.
DR OrthoDB; 1638924at2; -.
DR BioCyc; MetaCyc:MON-15968; -.
DR BRENDA; 1.20.1.1; 5158.
DR SABIO-RK; O69054; -.
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 InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Stress response.
FT CHAIN 1..336
FT /note="Phosphonate dehydrogenase"
FT /id="PRO_0000076033"
FT ACT_SITE 237
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 292
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:4E5N"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:4E5N"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4E5N"
FT TURN 212..216
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:4E5N"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:4E5N"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4E5N"
SQ SEQUENCE 336 AA; 36415 MW; 7F55D246CA4454F7 CRC64;
MLPKLVITHR VHDEILQLLA PHCELMTNQT DSTLTREEIL RRCRDAQAMM AFMPDRVDAD
FLQACPELRV VGCALKGFDN FDVDACTARG VWLTFVPDLL TVPTAELAIG LAVGLGRHLR
AADAFVRSGE FQGWQPQFYG TGLDNATVGI LGMGAIGLAM ADRLQGWGAT LQYHEAKALD
TQTEQRLGLR QVACSELFAS SDFILLALPL NADTQHLVNA ELLALVRPGA LLVNPCRGSV
VDEAAVLAAL ERGQLGGYAA DVFEMEDWAR ADRPRLIDPA LLAHPNTLFT PHIGSAVRAV
RLEIERCAAQ NIIQVLAGAR PINAANRLPK AEPAAC
