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Database: UniProt
Entry: S9V3Q2_9TRYP
LinkDB: S9V3Q2_9TRYP
Original site: S9V3Q2_9TRYP 
ID   S9V3Q2_9TRYP            Unreviewed;       395 AA.
AC   S9V3Q2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
GN   ORFNames=STCU_01111 {ECO:0000313|EMBL:EPY35563.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY35563.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY35563.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
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|RuleBase:RU003405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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:EPY35563.1}.
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DR   EMBL; ATMH01001111; EPY35563.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9V3Q2; -.
DR   EnsemblProtists; EPY35563; EPY35563; STCU_01111.
DR   OrthoDB; 145602at2759; -.
DR   Proteomes; UP000015354; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11540:SF48; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 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   Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|RuleBase:RU003405};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..209
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          211..381
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
SQ   SEQUENCE   395 AA;  42551 MW;  EAD3436495D6081D CRC64;
     MYCSSLSICM YITLFCYSVL FLSFFFSLCV YTTIDQKKKQ SLLLGTNGFF FRKKAEKKLG
     KVVVFGATTA VGQPLALLLK MCPHVRELVC CNTALDGPVP TVGVAADISH MDTDAQVRYA
     QDVNDWPAAL HEAQLVLVCS GANFDVLREH RDAALQATAP AMETVMRAVA TGAPSAAIGI
     VSSPVNALTP LCAEYLRREN KFDPRKLFGV TTLDVIRARR LVAKALAKNP YDVNVPVVGG
     RGGATACPLV AQTGLRLADE EIMHITMEVQ QYGSPFSEGR RSESTSLTTA VAPPVALGTA
     YAAYEFAVSV LKAQRGDYGI VECALVESTM RPETPFFSSR VELGAEGVER ILPMGRLTAF
     EEKLIDDAVA ELVKDVEAGM AYAKAGGPAK KTNED
//
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