ID A0A0R0DSH9_9GAMM Unreviewed; 327 AA.
AC A0A0R0DSH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:ALJ27320.1};
GN ORFNames=ABB33_09485 {ECO:0000313|EMBL:KRG85081.1}, AOT14_08890
GN {ECO:0000313|EMBL:ALJ27320.1};
OS Stenotrophomonas acidaminiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG85081.1, ECO:0000313|Proteomes:UP000050958};
RN [1] {ECO:0000313|EMBL:ALJ27320.1, ECO:0000313|Proteomes:UP000061010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ27320.1,
RC ECO:0000313|Proteomes:UP000061010};
RX PubMed=26659678;
RA Vinuesa P., Ochoa-Sanchez L.E.;
RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL Genome Announc. 3:e01433-15(2015).
RN [2] {ECO:0000313|EMBL:KRG85081.1, ECO:0000313|Proteomes:UP000050958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG85081.1,
RC ECO:0000313|Proteomes:UP000050958};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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(+) = 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: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}.
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DR EMBL; CP012900; ALJ27320.1; -; Genomic_DNA.
DR EMBL; LDJO01000026; KRG85081.1; -; Genomic_DNA.
DR RefSeq; WP_054663379.1; NZ_RZNW01000033.1.
DR AlphaFoldDB; A0A0R0DSH9; -.
DR KEGG; sacz:AOT14_08890; -.
DR PATRIC; fig|128780.6.peg.900; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000050958; Unassembled WGS sequence.
DR Proteomes; UP000061010; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase 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_choloroplast_like; 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 PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT DOMAIN 5..154
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 159..319
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 11..17
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 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 107
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 114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT BINDING 131..133
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 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 327 AA; 34838 MW; 9DC3CB23D0EB456F CRC64;
MKAPVRVAVT GAAGNIGYAL LFRIASGEML GKDQPVILQL LEIDNEKAQA ALKGVVMELE
DCAFPLLAGV VTTADPLVAF KDVDVALLVG ARPRGPGMER KDLLLENAKI FTVQGKALNA
VAKRDVKVLV VGNPANTNAY IAMKSAPDLD PKNFTAMLRL DHNRALSQLS AKTGKAVDSF
EKFTVWGNHS PTMYPDYRFA TTGGASVAEL INDQEWNANT FIPTVGKRGA AIIAARGLSS
AASAANAAID HVHDWVLGSN GKWVTMGVPS DGSYGIPEGV VFGFPVITEN GKYTIVKDLP
IDDFSKKYID ITLGELEEER AGVADLL
//