ID G8C2B5_TETPH Unreviewed; 391 AA.
AC G8C2B5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN Name=TPHA0P01350 {ECO:0000313|EMBL:CCE66293.1};
GN OrderedLocusNames=TPHA_0P01350 {ECO:0000313|EMBL:CCE66293.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE66293.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE66293.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
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DR EMBL; HE612871; CCE66293.1; -; Genomic_DNA.
DR RefSeq; XP_003688727.1; XM_003688679.1.
DR AlphaFoldDB; G8C2B5; -.
DR STRING; 1071381.G8C2B5; -.
DR GeneID; 11530899; -.
DR KEGG; tpf:TPHA_0P01350; -.
DR eggNOG; KOG1494; Eukaryota.
DR HOGENOM; CLU_047181_1_0_1; -.
DR OMA; GPPECAY; -.
DR OrthoDB; 5059897at2759; -.
DR Proteomes; UP000005666; Chromosome 16.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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 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; IPR010097; Malate_DH_type1.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 27..172
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 187..391
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 33..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 160..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 391 AA; 42195 MW; C86DDE1DD007722E CRC64;
MPVPAIEIID NPSVAHNDGD SRNATRVKVS VVGAGGGIGQ SLSLLLKVNL NNLLANDPSA
NASIELSLFD VNLENLKGVT ADLSHINNKI RLQVTDNLAE NVKDSNLIII AAGVPRKPGM
TRDDLFNINA GIIKNIATDI NNANACNSQN SGNSSFILLI SNPLNSLLPV LQNSLNENWI
GKCFGITELD LVRASTFLEP LLQSNSGNNA EMPYIPVIGG HSGDTILPVF SQITANNFTS
SLYDLVRGPD SQIIRKLINR VQYGGDEIVE AKNGKGSATL SMAYSAYRIA EQFTALLLNQ
VKTVESILYT TIVGKDFETP LSTVEGAAEL HDQYLERRLK FFATACTVEK LSGLTKIDNK
IIGNLNAFEK DNLLPTCIDS LQINIEKGLS F
//