ID   A0A078AHB7_STYLE        Unreviewed;       883 AA.
AC   A0A078AHB7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:CDW81236.1};
GN   Name=Contig5733.g6130 {ECO:0000313|EMBL:CDW81236.1};
GN   ORFNames=STYLEM_10249 {ECO:0000313|EMBL:CDW81236.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW81236.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW81236.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW81236.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   EMBL; CCKQ01009727; CDW81236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078AHB7; -.
DR   EnsemblProtists; CDW81236; CDW81236; STYLEM_10249.
DR   InParanoid; A0A078AHB7; -.
DR   OrthoDB; 501358at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0016615; F:malate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   CDD; cd01338; MDH_choloroplast_like; 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_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR010736; SHIPPO-rpt.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   Pfam; PF07004; SHIPPO-rpt; 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   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   DOMAIN          31..177
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          181..348
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   REGION          481..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  100067 MW;  7B1269DABA969E1F CRC64;
     MLSKVFKQLN KTQLTSVASR SMATHSDKPK RIVVTGAAGQ ISYSVLFRLA SGAFLGPNQR
     VILHLLDLPN MEEVLKGVQA ELHDCAFPLL DDVVITSNQA VAFKDVDYAY LVGAKPRGPG
     MERGDLLKDN GKIFVDTGKA INDNASRDCK VIVVGNPANT NCLIAQHYAK DIPRENFTAM
     TRLDHNRALT QLALKTGSRV TDIKNLVVWG NHSPTMYPDI RNTTVNGKKA TELVDSNWIE
     TEFTPRVQQR GAEIIKLRKL SSAASAGNAA IDHMRDWVNG SDEMQSISFY SDGKTYGVPE
     GLIFSFPVTT KNGKYEVIKG LNLDDEVSRT RIKKTTDELL SERQAVEHLL KMQDLFSYNK
     QLAGTPGPGQ YYDTQNITTN QSTLTSTKLF ENRPNMLPGV SIGKKKQCLS LYCAQNCCSI
     FNTARSHLTQ DILDGEILVK NESAAKLRNV GPGAYDVSQV KGQSFNIRTS DAFHQIYKET
     FRRHASNSRN PTQDRSLSSN RNDQKHSEST SYNKTKELIN SFFRKDKIES PPRKPIINHY
     RQASKSSIKD LKSKETLTNS IKKNQGNYAH RVSKKQNDDS PDSRVKLSTI SPIGSIKSKN
     KQLSQSPYVN NRDQQKFQTS LKKPPLSKLT RNNNQTQIVS DFRTQYSQNH EYQDRYDQSK
     MIKRETSLET KNQNKSQRIS IFEVNQDHND NNKTKKQNKQ KPKPKVQQQS LTKYEINSQN
     INDLTFDNEK NSSSKQSAFL LNKNKLSKFL QISDNQEEIK ASTETSSVNY AQIIMNNLNH
     KKNKNTQRIV LPLYAEFETN LRNDQIESSY YDSCNIPNDD SYTSSAAINS QFREPDIIDE
     HSQERRINPT DIRETFIVNR NDKNKFNSSS SFITSISQPM RHQ
//