ID LDH3_BACHK Reviewed; 316 AA. AC Q6HBQ8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 16-JUN-2009, entry version 40. DE RecName: Full=L-lactate dehydrogenase 3; DE Short=L-LDH 3; DE EC=1.1.1.27; GN Name=ldh3; OrderedLocusNames=BT9727_4708; OS Bacillus thuringiensis subsp. konkukian. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH 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; AE017355; AAT63957.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_039018.1; -. DR GeneID; 2853614; -. DR GenomeReviews; AE017355_GR; BT9727_4708. DR KEGG; btk:BT9727_4708; -. DR HOGENOM; Q6HBQ8; -. DR BioCyc; BTHU281309:BT9727_4708-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:HAMAP. DR GO; GO:0019642; P:anaerobic glycolysis; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00488; -; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT CHAIN 1 316 L-lactate dehydrogenase 3. FT /FTId=PRO_0000237543. FT NP_BIND 14 42 NAD (By similarity). FT ACT_SITE 178 178 Proton acceptor. FT BINDING 91 91 Substrate (By similarity). FT BINDING 123 123 NAD or substrate (By similarity). FT BINDING 154 154 Substrate (By similarity). FT BINDING 233 233 Substrate (By similarity). SQ SEQUENCE 316 AA; 34798 MW; CE4B64686E72E1DF CRC64; MKRHTRKIAI IGTGLVGSSC AYSIVNQGIC EELLLIDINH ERAVGEAMDL SHCINFTNTR TKVYAGSYED CKDMDIVIIT AGPAPKPGQS RLDTLGASAK IMESVVGGVM ESGFDGIFLL ASNPVDIITY QVWKLSGLPR NRVIGTGTSL DSSRLRTILS EMLHVDPRSI HGYSLGEHGD SQMVAWSHVT VGGKPILQIL EEQKERFGEI DLDEIVEKTA KAGWEIYKRK GTTYYGIGNS LAYIANSIFN DDHRVIAVSA ILDGEYGEYD ICTGVPAIIT RDGIREIVEL NLTEDEESRF AKSNDILRDY MKTIGY //