MDH_SALRD
ID MDH_SALRD Reviewed; 314 AA.
AC Q2S289;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487}; OrderedLocusNames=SRU_1571;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR EMBL; CP000159; ABC45135.1; -; Genomic_DNA.
DR RefSeq; WP_011404318.1; NC_007677.1.
DR RefSeq; YP_445692.1; NC_007677.1.
DR PDB; 3NEP; X-ray; 1.55 A; X=1-314.
DR PDBsum; 3NEP; -.
DR AlphaFoldDB; Q2S289; -.
DR SMR; Q2S289; -.
DR STRING; 309807.SRU_1571; -.
DR EnsemblBacteria; ABC45135; ABC45135; SRU_1571.
DR GeneID; 61496174; -.
DR KEGG; sru:SRU_1571; -.
DR PATRIC; fig|309807.25.peg.1625; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_10; -.
DR OMA; AWSHVTI; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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..314
FT /note="Malate dehydrogenase"
FT /id="PRO_0000241967"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:3NEP"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:3NEP"
FT HELIX 284..309
FT /evidence="ECO:0007829|PDB:3NEP"
SQ SEQUENCE 314 AA; 33256 MW; FD2F7BDA3F8249E8 CRC64;
MKVTVIGAGN VGATVAECVA RQDVAKEVVM VDIKDGMPQG KALDMRESSP IHGFDTRVTG
TNDYGPTEDS DVCIITAGLP RSPGMSRDDL LAKNTEIVGG VTEQFVEGSP DSTIIVVANP
LDVMTYVAYE ASGFPTNRVM GMAGVLDTGR FRSFIAEELD VSVRDVQALL MGGHGDTMVP
LPRYTTVGGI PVPQLIDDAR IEEIVERTKG AGGEIVDLMG TSAWYAPGAA AAEMTEAILK
DNKRILPCAA YCDGEYGLDD LFIGVPVKLG AGGVEEVIEV DLDADEKAQL KTSAGHVHSN
LDDLQRLRDE GKIG
