ID MDH_HALVD Reviewed; 304 AA. AC Q9P9L2; D4GYB6; Q0MSE3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 2. DT 27-MAR-2024, entry version 118. DE RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349}; DE EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349}; GN Name=mdh; OrderedLocusNames=HVO_3007; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales; OC Haloferacaceae; Haloferax. OX NCBI_TaxID=309800; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Mevarech M.; RT "The gene coding for Haloferax volcanii malate dehydrogenase."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RA Tetsch L., Galinski E.A.; RT "Expression of halophilic malate dehydrogenase of Haloferax volcanii."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). 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; AF236112; AAF43044.1; -; Genomic_DNA. DR EMBL; DQ851095; ABH10498.1; -; Genomic_DNA. DR EMBL; CP001956; ADE04975.1; -; Genomic_DNA. DR RefSeq; WP_004044925.1; NZ_AOHU01000104.1. DR PDB; 4BGU; X-ray; 1.49 A; A/B/C/D=2-304. DR PDBsum; 4BGU; -. DR AlphaFoldDB; Q9P9L2; -. DR SMR; Q9P9L2; -. DR STRING; 309800.HVO_3007; -. DR PaxDb; 309800-C498_18200; -. DR EnsemblBacteria; ADE04975; ADE04975; HVO_3007. DR GeneID; 8925993; -. DR KEGG; hvo:HVO_3007; -. DR eggNOG; arCOG00246; Archaea. DR HOGENOM; CLU_045401_1_1_2; -. DR OrthoDB; 2596at2157; -. DR Proteomes; UP000008243; 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 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 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; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; NF041314; Malate_DH_Halo; 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; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..304 FT /note="Malate dehydrogenase" FT /id="PRO_0000113483" FT ACT_SITE 176 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 8..14 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 83 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 96 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 119..121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:O08349" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P61889" FT CONFLICT 17 FT /note="A -> G (in Ref. 1; AAF43044)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="Missing (in Ref. 1; AAF43044)" FT /evidence="ECO:0000305" FT CONFLICT 290 FT /note="D -> N (in Ref. 1; AAF43044)" FT /evidence="ECO:0000305" FT CONFLICT 297 FT /note="R -> L (in Ref. 1; AAF43044)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 12..24 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 39..53 FT /evidence="ECO:0007829|PDB:4BGU" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 89..108 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 123..132 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 146..161 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 198..216 FT /evidence="ECO:0007829|PDB:4BGU" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 224..238 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 244..253 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 258..269 FT /evidence="ECO:0007829|PDB:4BGU" FT STRAND 272..276 FT /evidence="ECO:0007829|PDB:4BGU" FT HELIX 283..303 FT /evidence="ECO:0007829|PDB:4BGU" SQ SEQUENCE 304 AA; 32654 MW; 7AD72EDC9C137268 CRC64; MTKVSVIGAA GTVGAAAGYN LALRDVCDEL VFVDIPKMED KTVGQAADTN HGIAYDSNTV VTQGGYEDTA GSDVVVITAG IPRQPGQTRI DLAGDNAPIM DDIGSSLAEY NDDFVSITTS NPVDLLNRHL YETGDRDRHK VIGFGGRLDS ARFRYVLSQR FDVPVKNVDA TILGEHGDAQ VPVFSKVRVD GNDPAFSADE KEEILGDLQE SAMDVIERKG ATQWGPATGV AHMVEAVLHD TGEVLPGSLV LDGEFGYEDT AFGVPVKLGS NGIEEVVEWD LDDYEADLMD DAAEKLRDQY DEIA //