MDH_PICTO
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 03-AUG-2022, entry version 114.
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).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
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}.
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DR EMBL; AE017261; AAT43579.1; -; Genomic_DNA.
DR RefSeq; WP_011177795.1; NC_005877.1.
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 EnsemblBacteria; AAT43579; AAT43579; 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 OMA; ASCAEYI; -.
DR OrthoDB; 69007at2157; -.
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; -; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome;
KW 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
