ID A0A1E5DZH8_9VIBR Unreviewed; 311 AA.
AC A0A1E5DZH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01516};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01516};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516};
GN ORFNames=A1QC_12960 {ECO:0000313|EMBL:OEF22983.1};
OS Vibrio rumoiensis 1S-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF22983.1, ECO:0000313|Proteomes:UP000094070};
RN [1] {ECO:0000313|EMBL:OEF22983.1, ECO:0000313|Proteomes:UP000094070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1S-45 {ECO:0000313|EMBL:OEF22983.1,
RC ECO:0000313|Proteomes:UP000094070};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_01516}.
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|ARBA:ARBA00000774, ECO:0000256|HAMAP-
CC Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01516}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824, ECO:0000256|HAMAP-Rule:MF_01516}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEF22983.1}.
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DR EMBL; AJYK02000102; OEF22983.1; -; Genomic_DNA.
DR RefSeq; WP_017026338.1; NZ_AJYK02000102.1.
DR AlphaFoldDB; A0A1E5DZH8; -.
DR STRING; 1188252.A1QC_12960; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000094070; Unassembled WGS sequence.
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 CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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_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 NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01516,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000094070};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_01516}.
FT DOMAIN 1..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..309
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 311 AA; 32161 MW; EDEDCA3F48719363 CRC64;
MKVAVIGAAG GIGQALALLL KNGLPAGSDL ALYDIAPVTP GVAADLSHIP TPVSIKGYAG
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIIKS LAEKIAVTCP TACVGIITNP
VNTTVPIAAE VLKKAGVYNK HRLFGITTLD VIRSETFVSE LKGVSLEGLE VPVIGGHSGV
TILPLLSQVK GVEFTAEETA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA AYRFGLSLVK
ALQGEQGIIE CAYVEGDGEH ARFFAQPIRL GTEGVEEILS YGELSSFEQE AFDSMLDTLK
SDIALGEEFA K
//
