ID MDH_PYRHO Reviewed; 360 AA. AC O59028; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; GN Name=mdh; OrderedLocusNames=PH1277; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000001; BAA30380.1; -; Genomic_DNA. DR PIR; B71073; B71073. DR RefSeq; WP_010885364.1; NC_000961.1. DR PDB; 1V9N; X-ray; 2.10 A; A=1-360. DR PDBsum; 1V9N; -. DR AlphaFoldDB; O59028; -. DR SMR; O59028; -. DR STRING; 70601.gene:9378244; -. DR EnsemblBacteria; BAA30380; BAA30380; BAA30380. DR GeneID; 1443600; -. DR KEGG; pho:PH1277; -. DR eggNOG; arCOG04874; Archaea. DR OrthoDB; 40552at2157; -. DR EvolutionaryTrace; O59028; -. DR Proteomes; UP000000752; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 1.10.1530.10; -; 1. DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah. DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP. DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf. DR InterPro; IPR003767; Malate/L-lactate_DH-like. DR PANTHER; PTHR11091:SF0; HYDROXYCARBOXYLATE DEHYDROGENASE B-RELATED; 1. DR PANTHER; PTHR11091; OXIDOREDUCTASE-RELATED; 1. DR Pfam; PF02615; Ldh_2; 1. DR SUPFAM; SSF89733; L-sulfolactate dehydrogenase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..360 FT /note="Malate dehydrogenase" FT /id="PRO_0000083829" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 34..49 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 60..68 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 97..115 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 116..125 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 132..139 FT /evidence="ECO:0007829|PDB:1V9N" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:1V9N" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1V9N" FT TURN 223..227 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 242..256 FT /evidence="ECO:0007829|PDB:1V9N" FT TURN 257..261 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 278..285 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 293..308 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 324..336 FT /evidence="ECO:0007829|PDB:1V9N" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:1V9N" FT HELIX 342..355 FT /evidence="ECO:0007829|PDB:1V9N" SQ SEQUENCE 360 AA; 39751 MW; 6E9D8B16ECDE6E6F CRC64; MFEKGYVDEN YIRVPKDRLF SFIVRVLTKL GVPEEDAKIV ADNLVMADLR GVESHGVQRL KRYVDGIISG GVNLHPKIRV IREGPSYALI DGDEGLGQVV GYRSMKLAIK KAKDTGIGIV IARNSNHYGI AGYYALMAAE EGMIGISMTN SRPLVAPTGG IERILGTNPI ALAAPTKDKP FLLDMATSVV PIGKLEVYRR KGKDIPEGWA INREGNITTK VEEVFNGGAL LPLGGFGELL GGHKGYGLSL MVDILSGILS GGTWSKYVKN TSEKGSNVCH FFMVIDIEHF IPLEEFKEKI SQMIEEIKSS RKHPEFERIW IHGEKGFLTM ETRLKLGIPI YRKVLEELNE IAKRVGVEGL //