MDH_AQUAR
ID MDH_AQUAR Reviewed; 329 AA.
AC Q9ZF99;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
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};
OS Aquaspirillum arcticum.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Aquaspirillum.
OX NCBI_TaxID=87645;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123,
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=10206992; DOI=10.1074/jbc.274.17.11761;
RA Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y.;
RT "Structural basis for cold adaptation. Sequence, biochemical properties,
RT and crystal structure of malate dehydrogenase from a psychrophile
RT Aquaspirillium arcticum.";
RL J. Biol. Chem. 274:11761-11767(1999).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10206992}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000305}.
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DR EMBL; AF109682; AAD13225.1; -; Genomic_DNA.
DR PDB; 1B8P; X-ray; 1.90 A; A=1-329.
DR PDB; 1B8U; X-ray; 2.50 A; A=1-329.
DR PDB; 1B8V; X-ray; 2.10 A; A=1-329.
DR PDBsum; 1B8P; -.
DR PDBsum; 1B8U; -.
DR PDBsum; 1B8V; -.
DR AlphaFoldDB; Q9ZF99; -.
DR SMR; Q9ZF99; -.
DR DrugBank; DB02637; Oxaloacetate Ion.
DR PRIDE; Q9ZF99; -.
DR BRENDA; 1.1.1.37; 17133.
DR SABIO-RK; Q9ZF99; -.
DR EvolutionaryTrace; Q9ZF99; -.
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 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10206992"
FT CHAIN 2..329
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113346"
FT ACT_SITE 190
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 ECO:0000269|PubMed:10206992"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517,
FT ECO:0000269|PubMed:10206992"
FT BINDING 132..134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517,
FT ECO:0000269|PubMed:10206992"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517,
FT ECO:0000305|PubMed:10206992"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1B8P"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:1B8P"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1B8P"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 242..258
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:1B8P"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 304..324
FT /evidence="ECO:0007829|PDB:1B8P"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:1B8P"
SQ SEQUENCE 329 AA; 35251 MW; F02E2826E5028F27 CRC64;
MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ KALQGVMMEI
DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME RKDLLEANAQ IFTVQGKAID
AVASRNIKVL VVGNPANTNA YIAMKSAPSL PAKNFTAMLR LDHNRALSQI AAKTGKPVSS
IEKLFVWGNH SPTMYADYRY AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS
SAASAANAAI DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL
SIDAFSQERI NVTLNELLEE QNGVQHLLG
