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 16-JUN-2009, entry version 56. DE RecName: Full=D-lactate dehydrogenase; DE Short=D-LDH; DE EC=1.1.1.28; DE AltName: Full=D-specific D-2-hydroxyacid dehydrogenase; GN Name=ldhD; OrderedLocusNames=TP_0037; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; 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., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000520; AAC65033.1; -; Genomic_DNA. DR PIR; D71373; D71373. DR RefSeq; NP_218477.1; -. DR HSSP; P30901; 2DLD. DR IntAct; O83080; 1. DR GeneID; 2611300; -. DR GenomeReviews; AE000520_GR; TP_0037. DR KEGG; tpa:TP0037; -. DR NMPDR; fig|243276.1.peg.36; -. DR TIGR; TP_0037; -. DR HOGENOM; O83080; -. DR OMA; O83080; HAIAEHT. DR BioCyc; TPAL243276:TP_0037-MON; -. DR BRENDA; 1.1.1.28; 142600. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006139; D-isomer_2_OHA_DH. DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 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 Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 331 D-lactate dehydrogenase. FT /FTId=PRO_0000075971. FT ACT_SITE 235 235 By similarity. FT ACT_SITE 264 264 By similarity. FT ACT_SITE 296 296 Proton donor (By similarity). 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 //