ID   A0A1I8IIR3_9PLAT        Unreviewed;       642 AA.
AC   A0A1I8IIR3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Putative malate dehydrogenase 1B {ECO:0000256|ARBA:ARBA00039310};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0013240-snap-gene-0.3-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0013240-snap-gene-0.3-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   AlphaFoldDB; A0A1I8IIR3; -.
DR   WBParaSite; maker-uti_cns_0013240-snap-gene-0.3-mRNA-1; maker-uti_cns_0013240-snap-gene-0.3-mRNA-1; maker-uti_cns_0013240-snap-gene-0.3.
DR   Proteomes; UP000095280; Unplaced.
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; 1.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF1; MALATE DEHYDROGENASE 1B-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 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;
FT   DOMAIN          331..497
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   REGION          215..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..642
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  69897 MW;  65714AC0A20A738D CRC64;
     MAKIVIAGSA DCPYFAKVEL LADNLAKNLP SFKLHKIVRT ANDWPDWSRH CCRERGWRHQ
     RSPIIWRELV NQGGKGVLIG GANEFQEFAK AYYDAESSML SPEMLAVAKD NSRYKSELDA
     EEAHLRSLSK PLQVLVTASA SPTAYQLLPL LMDGSVFGRS TELAFTLFDC DGLVMEAFDL
     AHPLVRSIRA TANFQEAAAA ADILLLLDDV LLKPPSPQES ATDGEEDKKA AMATEASPAE
     GDSPTKLDKS DADAAASAAE LAARVDWLSA AAAVYRRYAD WLNAAECSRR LKVLLAGRGP
     VNFGARVLLD ACPRLPARNV AAAGRLLERQ AKGALAGHMK VLPSSVVDLI VWGDPAGENL
     VDLSRARVHY YDGSITGPDS YNQPVLDTVW DKKWLNQEFP KTMRQRQDNN LLLGGTGPRS
     AALSTAQATA DTVRNWWLGG SGNEICSLGV VSEGWYGIPP GRVFSFPVRF QPKGAWSVVE
     DVDLSEESVQ RLAQLAEAAQ RDYLLVFPPP KPPTPEPVVE ESVDIGGDLE IALDDGQKVP
     SQTPVDMASV EQLRDRLQSL SLPALSAEAL LKLTPDLVEQ LLRLEDVEQL RARLQRLEEA
     PLTTVAEEVG DAQAADDAEA EAEEENNDEV NEEEEAGEEG DD
//