MDH_MYCTU
ID MDH_MYCTU Reviewed; 329 AA.
AC P9WK13; L0T626; O54592; P0A5J6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=Rv1240;
GN ORFNames=MTV006.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01517};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR EMBL; AL123456; CCP43996.1; -; Genomic_DNA.
DR PIR; G70952; G70952.
DR RefSeq; NP_215756.1; NC_000962.3.
DR RefSeq; WP_003406301.1; NZ_NVQJ01000039.1.
DR PDB; 4TVO; X-ray; 1.50 A; A/B=2-329.
DR PDB; 5KVV; X-ray; 2.01 A; A/B=2-329.
DR PDBsum; 4TVO; -.
DR PDBsum; 5KVV; -.
DR AlphaFoldDB; P9WK13; -.
DR SMR; P9WK13; -.
DR STRING; 83332.Rv1240; -.
DR PaxDb; P9WK13; -.
DR DNASU; 887119; -.
DR GeneID; 45425210; -.
DR GeneID; 887119; -.
DR KEGG; mtu:Rv1240; -.
DR TubercuList; Rv1240; -.
DR eggNOG; COG0039; Bacteria.
DR OMA; TKGMERG; -.
DR PhylomeDB; P9WK13; -.
DR BioCyc; MetaCyc:G185E-5411-MON; -.
DR BRENDA; 1.1.1.37; 3445.
DR SABIO-RK; P9WK13; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:MTBBASE.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:MTBBASE.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MTBBASE.
DR Gene3D; 3.90.110.10; -; 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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
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; TIGR01759; MalateDH-SF1; 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..329
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113380"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 12..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 130..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:4TVO"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:4TVO"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:4TVO"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5KVV"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:4TVO"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:4TVO"
FT HELIX 303..325
FT /evidence="ECO:0007829|PDB:4TVO"
SQ SEQUENCE 329 AA; 34322 MW; 0A512659617F9C37 CRC64;
MSASPLKVAV TGAAGQIGYS LLFRLASGSL LGPDRPIELR LLEIEPALQA LEGVVMELDD
CAFPLLSGVE IGSDPQKIFD GVSLALLVGA RPRGAGMERS DLLEANGAIF TAQGKALNAV
AADDVRVGVT GNPANTNALI AMTNAPDIPR ERFSALTRLD HNRAISQLAA KTGAAVTDIK
KMTIWGNHSA TQYPDLFHAE VAGKNAAEVV NDQAWIEDEF IPTVAKRGAA IIDARGASSA
ASAASATIDA ARDWLLGTPA DDWVSMAVVS DGSYGVPEGL ISSFPVTTKG GNWTIVSGLE
IDEFSRGRID KSTAELADER SAVTELGLI
