MDHM_FELCA
ID MDHM_FELCA Reviewed; 338 AA.
AC K0J107; Q0QF33;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Malate dehydrogenase, mitochondrial {ECO:0000255|RuleBase:RU003405, ECO:0000303|PubMed:25177965};
DE EC=1.1.1.37 {ECO:0000255|RuleBase:RU003405};
DE Flags: Precursor;
GN Name=MDH2 {ECO:0000303|PubMed:25177965};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1] {ECO:0000312|EMBL:BAM48565.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000303|PubMed:25177965};
RX PubMed=25177965; DOI=10.4238/2014.august.29.7;
RA Sasaki N., Nakamura M., Soeta S.;
RT "Molecular analysis of cytosolic and mitochondrial malate dehydrogenases
RT isolated from domestic cats (Felis catus).";
RL Genet. Mol. Res. 13:6855-6864(2014).
RN [2] {ECO:0000312|Ensembl:ENSFCAP00000000558, ECO:0000312|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000312|Ensembl:ENSFCAP00000000558,
RC ECO:0000312|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [3] {ECO:0000312|EMBL:ABD77294.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-314.
RX PubMed=16751257; DOI=10.1093/molbev/msl027;
RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL Mol. Biol. Evol. 23:1493-1503(2006).
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|RuleBase:RU003405};
CC -!- ACTIVITY REGULATION: Enzyme activity is enhanced by acetylation.
CC {ECO:0000250|UniProtKB:P40926}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00346}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P04636}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC skeletal muscle and heart. Also expressed in liver, ileum, colon,
CC kidney and adipose tissue, and at very low levels in lung, pancreas,
CC stomach and spleen. {ECO:0000269|PubMed:25177965}.
CC -!- PTM: Acetylation is enhanced after treatment either with trichostin A
CC (TSA) or with nicotinamide (NAM) with the appearance of tri- and
CC tetraacetylations. Glucose also increases acetylation.
CC {ECO:0000250|UniProtKB:P40926}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000255|RuleBase:RU003369, ECO:0000305}.
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DR EMBL; AB751611; BAM48565.1; -; mRNA.
DR EMBL; AANG02069421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ402961; ABD77294.1; -; mRNA.
DR RefSeq; NP_001265782.1; NM_001278853.1.
DR AlphaFoldDB; K0J107; -.
DR SMR; K0J107; -.
DR STRING; 9685.ENSFCAP00000000558; -.
DR Ensembl; ENSFCAT00000000600; ENSFCAP00000000558; ENSFCAG00000000600.
DR GeneID; 101084845; -.
DR KEGG; fca:101084845; -.
DR CTD; 4191; -.
DR VGNC; VGNC:68221; MDH2.
DR eggNOG; KOG1494; Eukaryota.
DR GeneTree; ENSGT00390000016686; -.
DR HOGENOM; CLU_047181_0_1_1; -.
DR InParanoid; K0J107; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 976445at2759; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000000600; Expressed in adult mammalian kidney and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 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; 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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Glycoprotein; Mitochondrion; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00346"
FT CHAIN 25..338
FT /note="Malate dehydrogenase, mitochondrial"
FT /id="PRO_0000438644"
FT ACT_SITE 173
FT /note="Proton relay"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-1"
FT BINDING 31..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 140..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 185
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 185
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 203
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 215
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 215
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 239
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 269
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 296
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 296
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 301
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 301
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 307
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 307
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 307
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 314
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 314
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 324
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 324
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 328
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 328
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 329
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 329
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q32LG3"
FT MOD_RES 335
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 335
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08249"
FT CARBOHYD 33
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P04636"
FT CONFLICT 26
FT /note="K -> N (in Ref. 3; ABD77294)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="P -> S (in Ref. 3; ABD77294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 35514 MW; 72B6568900E28FA6 CRC64;
MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH
TPGVAADLSH IETRAAVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNASI
VATLTAACAQ HCPEAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF
IAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDLPQ DQLTAVTGRI QEAGTEVVKA
KAGAGSATLS MAYAGARFVF SLVDAINGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE
KNLGIGKISP FEEKMIAEAL PELKASIKKG EEFVKNMK
