ID MDH_PICTO Reviewed; 324 AA. AC Q6L0C3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349}; DE EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349}; GN Name=mdh; OrderedLocusNames=PTO0994; OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC OS 100828 / KAW 2/3). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Picrophilaceae; Picrophilus. OX NCBI_TaxID=1122961; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3; RX PubMed=15184674; DOI=10.1073/pnas.0401356101; RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., RA Schepers B., Dock C., Antranikian G., Liebl W.; RT "Genome sequence of Picrophilus torridus and its implications for life RT around pH 0."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000250|UniProtKB:O08349}. 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 Evidence={ECO:0000250|UniProtKB:O08349}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {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; AE017261; AAT43579.1; -; Genomic_DNA. DR RefSeq; WP_011177795.1; NZ_FWYE01000003.1. DR PDB; 4BGV; X-ray; 1.81 A; A/B/C/D=2-324. DR PDBsum; 4BGV; -. DR AlphaFoldDB; Q6L0C3; -. DR SMR; Q6L0C3; -. DR STRING; 263820.PTO0994; -. DR PaxDb; 263820-PTO0994; -. DR GeneID; 2844444; -. DR KEGG; pto:PTO0994; -. DR PATRIC; fig|263820.9.peg.1033; -. DR eggNOG; arCOG00246; Archaea. DR HOGENOM; CLU_045401_2_1_2; -. DR InParanoid; Q6L0C3; -. DR OrthoDB; 2596at2157; -. DR Proteomes; UP000000438; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR CDD; cd01339; LDH-like_MDH; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00487; Malate_dehydrog_3; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR011275; Malate_DH_type3. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01763; MalateDH_bact; 1. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 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 SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..324 FT /note="Malate dehydrogenase" FT /id="PRO_0000113490" FT ACT_SITE 181 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 124..126 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 126 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 13..24 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 28..36 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 39..48 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 68..74 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 94..115 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 128..139 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 151..166 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 173..179 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 185..194 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 205..216 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 218..226 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 233..247 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 252..260 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 263..268 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 272..282 FT /evidence="ECO:0007829|PDB:4BGV" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:4BGV" FT HELIX 296..322 FT /evidence="ECO:0007829|PDB:4BGV" SQ SEQUENCE 324 AA; 35215 MW; 86937A7F6AC89D4C CRC64; MARSKISVIG AGAVGATVAQ TLAIRQTGDI YIFDIVDGLA EGKALDILEG APHWGYDLDI KGFCTADESK YAEMKGSDVI VVTAGLARKP GMSRDDLLLK NIGIMKSVGE AIKKYSPESK IVVVTNPADI MAYAIYKASG ISPERIIGLG GSLDSTRFRT FLAQELNVSF EDVNAFVIGG HGDDMVPFIR YSNVSGIPIE DLLPREKIDE IVKRTRFGGG EIVNLYKTGS AFYAPGISIA VMVESIVNDR KRVIPCAAYI TGEHSKTYLV NNLFIGVPIK IGKNGVEKIY DLKFNEDELE AWKKSVESVK KNSAIADDYF AKNQ //