LDHD_TREPA
ID LDHD_TREPA Reviewed; 331 AA.
AC O83080;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=D-lactate dehydrogenase;
DE Short=D-LDH;
DE EC=1.1.1.28;
DE AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
GN Name=ldhD; OrderedLocusNames=TP_0037;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:16369, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.28;
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AE000520; AAC65033.1; -; Genomic_DNA.
DR PIR; D71373; D71373.
DR RefSeq; WP_010881486.1; NC_021490.2.
DR PDB; 7JP2; X-ray; 1.38 A; A/B=1-331.
DR PDBsum; 7JP2; -.
DR AlphaFoldDB; O83080; -.
DR SMR; O83080; -.
DR IntAct; O83080; 1.
DR STRING; 243276.TPANIC_0037; -.
DR EnsemblBacteria; AAC65033; AAC65033; TP_0037.
DR GeneID; 57878579; -.
DR KEGG; tpa:TP_0037; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_12; -.
DR OMA; PHIAWAY; -.
DR OrthoDB; 1638924at2; -.
DR BRENDA; 1.1.1.28; 6429.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..331
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075971"
FT ACT_SITE 235
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 264
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 296
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 156..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 206..207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 233..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:7JP2"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:7JP2"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:7JP2"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:7JP2"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:7JP2"
FT HELIX 302..320
FT /evidence="ECO:0007829|PDB:7JP2"
SQ SEQUENCE 331 AA; 36873 MW; 773B01E6E2384E0A CRC64;
MRCVVFNLRE EEAPYVEKWK QSHPGVVVDT YEEPLTAKNK ELLKGYEGLV VMQFLAMEDE
VYDYMGACKL KVLSTRTAGF DMYNATLLKK HGIRLTNVPS YSPNAIGEYA LAAALQLTRH
AREIETFVRK RDFRWQKPIL SKELRCSRVG ILGTGRIGQA AARLFKGVGA QVVGFDPYPN
DAAKEWLTYV SMDELLSTSD VISLHMPATK DSHHLINAKT IAQMKDGVYL VNTARGAVID
SQALLDSLDK GKIAGAALDA YEFEGPYIPK DNGNNPITDT VYARLVAHER IIYTPHIAFY
TETAIENMVF NSLDACTTVL RGEPCAAEIK L
