ID B4RCG7_PHEZH Unreviewed; 329 AA. AC B4RCG7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 02-SEP-2026, entry version 110. DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517, GN ECO:0000313|EMBL:ACG76566.1}; GN OrderedLocusNames=PHZ_c0152 {ECO:0000313|EMBL:ACG76566.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Caulobacterales; Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG76566.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG76566.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG76566.1, RC ECO:0000313|Proteomes:UP000001868}; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_01517}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = oxaloacetate + NADH + H(+); 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:0000256|HAMAP-Rule:MF_01517}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}. 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; CP000747; ACG76566.1; -; Genomic_DNA. DR RefSeq; WP_012520714.1; NC_011144.1. DR AlphaFoldDB; B4RCG7; -. DR STRING; 450851.PHZ_c0152; -. DR KEGG; pzu:PHZ_c0152; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_5; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000001868; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01338; MDH_chloroplast-like; 1. DR FunFam; 3.40.50.720:FF:000010; Malate dehydrogenase; 1. DR FunFam; 3.90.110.10:FF:000002; Malate dehydrogenase; 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_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01759; MalateDH-SF1; 1. DR NCBIfam; NF003916; PRK05442.1; 1. DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01517}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01517}; Reference proteome {ECO:0000313|Proteomes:UP000001868}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_01517}. FT DOMAIN 8..149 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 161..325 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 191 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 13..19 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 109 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 116 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517" FT BINDING 133..135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" SQ SEQUENCE 329 AA; 35030 MW; 7242962500431C36 CRC64; MASKPPIRVA VTGAAGNIGY ALLFRIASGE MLGKDQPVIL QLLEIPAEGP QKALKGVAME LEDCAFPLLQ DMVLTDDANV AFKDANWCLL VGSKPRGPGM ERADLLKDNG KIFIAQGKAI DAVAADDARV AVVGNPCNTN VMIAASQAKR LTPDRFTAMV RLDENRGRAQ LAKKAGVSIN DVSELFIYGN HSPTMFADFT HAKIGGKAAA DVINDRAWLE NEYLPTVGKR GAAIIEARGQ SSAASAANAL IDHVRSLNTV GEVHSIAVNS EGRYGFAEGV WAGMPVKTTA PGAYEVVTSY EMDDFAKSKI KITNDELVAE RDTVKDMLG //