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Database: UniProt
Entry: H2ISV7_RAHAC
LinkDB: H2ISV7_RAHAC
Original site: H2ISV7_RAHAC 
ID   H2ISV7_RAHAC            Unreviewed;       312 AA.
AC   H2ISV7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   OrderedLocusNames=Rahaq2_0492 {ECO:0000313|EMBL:AEX50426.1};
OS   Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS   NCIMB 13365 / CIP 78.65).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50426.1, ECO:0000313|Proteomes:UP000009010};
RN   [1] {ECO:0000313|EMBL:AEX50426.1, ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX   PubMed=22582378; DOI=10.1128/JB.00380-12;
RA   Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA   Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA   Tapia R., Woyke T., Sobecky P.A.;
RT   "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL   J. Bacteriol. 194:3020-3021(2012).
RN   [2] {ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA   Martinez R., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP003244; AEX50426.1; -; Genomic_DNA.
DR   RefSeq; WP_014333686.1; NZ_JMPO01000135.1.
DR   AlphaFoldDB; H2ISV7; -.
DR   STRING; 745277.Rahaq2_0492; -.
DR   GeneID; 61510634; -.
DR   KEGG; raq:Rahaq2_0492; -.
DR   PATRIC; fig|745277.3.peg.467; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_047181_1_0_6; -.
DR   OMA; MGWTSQA; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000009010; Chromosome.
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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01516}; Reference proteome {ECO:0000313|Proteomes:UP000009010};
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   312 AA;  32614 MW;  9B6E4910823FA22E CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFCG
     EDAKPALEGA DIVLISAGVA RKPGMDRSDL FNVNAGIVRN LIQQVASTCP KASIGIITNP
     VNTTVAIAAE VLKNAGVYDK NKLFGVTTLD TIRSNTFVAE LKGKQPEEIE VPVIGGHSGV
     TILPLLSQIS DVSFTESEIA ALTQRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     AMQGERNVVE CAYVEGKGDY ARFFAQPVLL GQNGIAELID IGQLSAFEQQ SLDSMLDILR
     KDIELGEQFI NK
//
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