MDH_HAEIN
ID MDH_HAEIN Reviewed; 311 AA.
AC P44427; Q7WRT7; Q83V59; Q83V60; Q99Q89; Q99Q90; Q99QA9; Q9AMQ2; Q9AMQ3;
AC Q9AMQ4; Q9AMQ5; Q9AMQ6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; OrderedLocusNames=HI_1210;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195.
RC STRAIN=1124, 1158, 1181, 1209, 375, 477, 667, 723, a1042, a6062, a6064,
RC a6073, a7190, a7205, b1324, b6107, b7017, b7109, b7651, b7717, Beagan,
RC c1271, c6132, c6134, c7424, c8032, d6137, Drm118, e6158, e6181, e6229,
RC e7066, f6237, f6252, f7283, and f7290;
RX PubMed=11136255; DOI=10.1073/pnas.98.1.182;
RA Feil E.J., Holmes E.C., Bessen D.E., Chan M.-S., Day N.P.J., Enright M.C.,
RA Goldstein R., Hood D.W., Kalia A., Moore C.E., Zhou J., Spratt B.G.;
RT "Recombination within natural populations of pathogenic bacteria: Short-
RT term empirical estimates and long-term phylogenetic consequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:182-187(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195.
RC STRAIN=1008, 1180, 1200, 1207, 1231, 1233, 1247, 1268, 162, 176, 285, 432,
RC 486, and 981;
RX PubMed=12797973; DOI=10.1016/s1567-1348(02)00152-1;
RA Cody A.J., Field D., Feil E.J., Stringer S., Deadman M.E., Tsolaki A.G.,
RA Gratz B., Bouchet V., Goldstein R., Hood D.W., Moxon E.R.;
RT "High rates of recombination in otitis media isolates of non-typeable
RT Haemophilus influenzae.";
RL Infect. Genet. Evol. 3:57-66(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195.
RC STRAIN=767, 769, 773, 788, 794, 795, 796, and 800;
RX PubMed=12843045; DOI=10.1128/jcm.41.7.3064-3069.2003;
RA O'Neill J.M., St Geme J.W. III, Cutter D., Adderson E.E., Anyanwu J.,
RA Jacobs R.F., Schutze G.E.;
RT "Invasive disease due to nontypeable Haemophilus influenzae among children
RT in Arkansas.";
RL J. Clin. Microbiol. 41:3064-3069(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195.
RC STRAIN=BR134, BR229, BR355, BR48, and BRC1-13;
RX PubMed=12800772;
RA Platonov A.E., Mironov K.O., Iatsyshina S.B., Koroleva I.S.,
RA Platonova O.V., Gushchin A.E., Shipulin G.A.;
RT "Multilocus sequence-typing for characterization of Moscow strains of
RT Haemophilus influenzae type b.";
RL Mol. Genet. Mikrobiol. Virusol. 2:21-25(2003).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22864.1; -; Genomic_DNA.
DR EMBL; AF322740; AAK11394.1; -; Genomic_DNA.
DR EMBL; AF322741; AAK11395.1; -; Genomic_DNA.
DR EMBL; AF322742; AAK11396.1; -; Genomic_DNA.
DR EMBL; AF322743; AAK11397.1; -; Genomic_DNA.
DR EMBL; AF322744; AAK11398.1; -; Genomic_DNA.
DR EMBL; AF322745; AAK11399.1; -; Genomic_DNA.
DR EMBL; AF322746; AAK11400.1; -; Genomic_DNA.
DR EMBL; AF322747; AAK11401.1; -; Genomic_DNA.
DR EMBL; AF322748; AAK11402.1; -; Genomic_DNA.
DR EMBL; AF322749; AAK11403.1; -; Genomic_DNA.
DR EMBL; AF322750; AAK11404.1; -; Genomic_DNA.
DR EMBL; AF322751; AAK11405.1; -; Genomic_DNA.
DR EMBL; AF322752; AAK11406.1; -; Genomic_DNA.
DR EMBL; AF322753; AAK11407.1; -; Genomic_DNA.
DR EMBL; AF322754; AAK11408.1; -; Genomic_DNA.
DR EMBL; AF322755; AAK11409.1; -; Genomic_DNA.
DR EMBL; AF322756; AAK11410.1; -; Genomic_DNA.
DR EMBL; AF322757; AAK11411.1; -; Genomic_DNA.
DR EMBL; AF322758; AAK11412.1; -; Genomic_DNA.
DR EMBL; AF322759; AAK11413.1; -; Genomic_DNA.
DR EMBL; AF322760; AAK11414.1; -; Genomic_DNA.
DR EMBL; AF322761; AAK11415.1; -; Genomic_DNA.
DR EMBL; AF322762; AAK11416.1; -; Genomic_DNA.
DR EMBL; AF322763; AAK11417.1; -; Genomic_DNA.
DR EMBL; AF322764; AAK11418.1; -; Genomic_DNA.
DR EMBL; AF322765; AAK11419.1; -; Genomic_DNA.
DR EMBL; AF322766; AAK11420.1; -; Genomic_DNA.
DR EMBL; AF322767; AAK11421.1; -; Genomic_DNA.
DR EMBL; AF322768; AAK11422.1; -; Genomic_DNA.
DR EMBL; AF322769; AAK11423.1; -; Genomic_DNA.
DR EMBL; AF322770; AAK11424.1; -; Genomic_DNA.
DR EMBL; AF322771; AAK11425.1; -; Genomic_DNA.
DR EMBL; AF322772; AAK11426.1; -; Genomic_DNA.
DR EMBL; AF322773; AAK11427.1; -; Genomic_DNA.
DR EMBL; AF322774; AAK11428.1; -; Genomic_DNA.
DR EMBL; AF322775; AAK11429.1; -; Genomic_DNA.
DR EMBL; AF322776; AAK11430.1; -; Genomic_DNA.
DR EMBL; AF536037; AAP19893.1; -; Genomic_DNA.
DR EMBL; AF536038; AAP19894.1; -; Genomic_DNA.
DR EMBL; AF536039; AAP19895.1; -; Genomic_DNA.
DR EMBL; AF536040; AAP19896.1; -; Genomic_DNA.
DR EMBL; AF536041; AAP19897.1; -; Genomic_DNA.
DR EMBL; AF536042; AAP19898.1; -; Genomic_DNA.
DR EMBL; AF536043; AAP19899.1; -; Genomic_DNA.
DR EMBL; AF536044; AAP19900.1; -; Genomic_DNA.
DR EMBL; AF536045; AAP19901.1; -; Genomic_DNA.
DR EMBL; AF536046; AAP19902.1; -; Genomic_DNA.
DR EMBL; AF536047; AAP19903.1; -; Genomic_DNA.
DR EMBL; AF536048; AAP19904.1; -; Genomic_DNA.
DR EMBL; AF536049; AAP19905.1; -; Genomic_DNA.
DR EMBL; AF536050; AAP19906.1; -; Genomic_DNA.
DR EMBL; AY245392; AAP74406.1; -; Genomic_DNA.
DR EMBL; AY245393; AAP74407.1; -; Genomic_DNA.
DR EMBL; AY245394; AAP74408.1; -; Genomic_DNA.
DR EMBL; AY245395; AAP74409.1; -; Genomic_DNA.
DR EMBL; AY245396; AAP74410.1; -; Genomic_DNA.
DR EMBL; AY245397; AAP74411.1; -; Genomic_DNA.
DR EMBL; AY245398; AAP74412.1; -; Genomic_DNA.
DR EMBL; AY245399; AAP74413.1; -; Genomic_DNA.
DR EMBL; AF525726; AAM91960.1; -; Genomic_DNA.
DR EMBL; AF525727; AAM91961.1; -; Genomic_DNA.
DR EMBL; AF525728; AAM91962.1; -; Genomic_DNA.
DR EMBL; AF525729; AAM91963.1; -; Genomic_DNA.
DR EMBL; AF525730; AAM91964.1; -; Genomic_DNA.
DR PIR; C64110; C64110.
DR RefSeq; NP_439366.1; NC_000907.1.
DR RefSeq; WP_005694235.1; NC_000907.1.
DR PDB; 6AOO; X-ray; 2.15 A; A/B=1-311.
DR PDB; 6BAL; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-311.
DR PDBsum; 6AOO; -.
DR PDBsum; 6BAL; -.
DR AlphaFoldDB; P44427; -.
DR SMR; P44427; -.
DR STRING; 71421.HI_1210; -.
DR PRIDE; P44427; -.
DR EnsemblBacteria; AAC22864; AAC22864; HI_1210.
DR KEGG; hin:HI_1210; -.
DR PATRIC; fig|71421.8.peg.1262; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_047181_0_1_6; -.
DR OMA; MGWTSQA; -.
DR PhylomeDB; P44427; -.
DR BioCyc; HINF71421:G1GJ1-1241-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..311
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113306"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VARIANT 63
FT /note="P -> L (in strain: 767 and 794)"
FT VARIANT 64
FT /note="T -> I (in strain: 432)"
FT VARIANT 66
FT /note="A -> T (in strain: 1124)"
FT VARIANT 107..108
FT /note="VT -> TI (in strain: 773, 796 and 1231)"
FT VARIANT 107
FT /note="V -> I (in strain: 162, 375, 723, 788, 800, 1008,
FT 1124, 1158, 1180, 1181, 1207, 1233, 1247, a6062, e6158,
FT e6229, e7066, f6237 and 1209)"
FT VARIANT 107
FT /note="V -> T (in strain: a7205, BR355 and e6181)"
FT VARIANT 128
FT /note="A -> V (in strain: c6132)"
FT VARIANT 135
FT /note="A -> S (in strain: a7205)"
FT VARIANT 163
FT /note="G -> D (in strain: f6252)"
FT VARIANT 193
FT /note="K -> E (in strain: 176, 667, a7205, b7017, c1271,
FT c6134, c7424 and c8032)"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 91..108
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6AOO"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:6BAL"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6BAL"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:6BAL"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:6BAL"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6BAL"
FT HELIX 285..309
FT /evidence="ECO:0007829|PDB:6BAL"
SQ SEQUENCE 311 AA; 32543 MW; 1311441B90E4EA2C CRC64;
MKVAVLGAAG GIGQALALLL KLQLPAGTDL SLYDIAPVTP GVAVDVSHIP TAVNVKGFSG
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRG LIEKVAVTCP KACVGIITNP
VNTTVAIAAE VLKKAGVYDK RKLFGVTTLD VLRSETFVAE LKGLNVSRTS VPVIGGHSGV
TILPLLSQVQ YAKWNEDEIE PLTKRIQNAG TEVLNAKAGG GSATLSMAQA AARFARSLVK
GLSGETVVEC TYVEGDGKYA RFFSQPVRLG KEGVEEILPI GPLSNFEQQA LENMLPTLRA
DIELGEKFIN G
