ID K9TQZ6_9CYAN Unreviewed; 327 AA.
AC K9TQZ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN ORFNames=Oscil6304_5304 {ECO:0000313|EMBL:AFY84793.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY84793.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY84793.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY84793.1,
RC ECO:0000313|Proteomes:UP000010367};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
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_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR EMBL; CP003607; AFY84793.1; -; Genomic_DNA.
DR RefSeq; WP_015151405.1; NC_019693.1.
DR AlphaFoldDB; K9TQZ6; -.
DR STRING; 56110.Oscil6304_5304; -.
DR KEGG; oac:Oscil6304_5304; -.
DR PATRIC; fig|56110.3.peg.6504; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_3; -.
DR InParanoid; K9TQZ6; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000010367; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_00487, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000010367};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00487}.
FT DOMAIN 15..153
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 158..319
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 20..25
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 129..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 327 AA; 35268 MW; C12ABDDD594B53E1 CRC64;
MSSSPFFPRS CHQARVSIIG AGKVGSTLAQ RVAEKNLADV VMLDVLEGMP QGLALDLMEA
RGVEGHDRQI IGTNDYDDTA NSDIVVITAG RPRKPGMNRD DLIEINAKIV KTAAKEAVAR
SPEAILIVVT NPLDVMTYVA WEASQLPCRR VIGMAGVLDA ARFKTFISME LGVSIQDIKA
MVLGDHGQLM VPLPRYTTVD GIPLMELMDT QTIERIVERT RNGGTEIVEL MKTGSAYFAP
ASSVSLMIEA ILLDQSRIVP AAAYLQGEYG LRDLFIGVPC QLGCQGITQV LELELDEGER
AAFQASAESV AQHLKQAKEI LSGSTLG
//
