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Database: UniProt
Entry: X6M8R9_RETFI
LinkDB: X6M8R9_RETFI
Original site: X6M8R9_RETFI 
ID   X6M8R9_RETFI            Unreviewed;       436 AA.
AC   X6M8R9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ETO09405.1};
DE   Flags: Fragment;
GN   ORFNames=RFI_27971 {ECO:0000313|EMBL:ETO09405.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO09405.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO09405.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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:ETO09405.1}.
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DR   EMBL; ASPP01024084; ETO09405.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6M8R9; -.
DR   EnsemblProtists; ETO09405; ETO09405; RFI_27971.
DR   OrthoDB; 501358at2759; -.
DR   Proteomes; UP000023152; 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   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; 2.
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   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT   DOMAIN          199..270
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          274..310
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   DOMAIN          326..435
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         436
FT                   /evidence="ECO:0000313|EMBL:ETO09405.1"
SQ   SEQUENCE   436 AA;  47980 MW;  15875FBB3909F577 CRC64;
     MSTGLSKEDT ILPRNDRKTK EELNERNSAL SQIHKELQSV RKELLVSGCA LTAATFRSAA
     RKYLLGVREE VDYLRQHRFA RTLIKEPLRV VITGAAGQVG YALVPLVASG QVLGLDQPLI
     LTLLEIPSAL KALNGVAMEI EDGAYPLVDA VIPTTDPAVK EEGEKERERG FEKGNKKKYK
     TIDSSFCCIT IFFLKYYYVD YAILVGGFPR GVGMERKDLL AKNAPIFQSM GEGLQKYAKE
     TCKVLVVANP ANTNCLTCSR HATKIPRRNF AALTRLDQNR ATVQLAHKLG VPVRAVSNVA
     IWGNHSNTQL HFLFLFFFDT LQNSISSFQV PDVSHAVVAV DGVQKKAEVE EKWVSGEFIP
     SVQQRGKAVL EARNSSSAVS AANAIKDAIR DWHFGTPEGA HVALAVYSDG SHYGVAKDIF
     FSFPVTCKNG TYTIVS
//
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