ID   A0A183B0T5_9TREM        Unreviewed;       525 AA.
AC   A0A183B0T5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Putative malate dehydrogenase 1B {ECO:0000256|ARBA:ARBA00039310};
GN   ORFNames=ECPE_LOCUS12819 {ECO:0000313|EMBL:VDP90091.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001285701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0001285701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP90091.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP90091.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UZAN01053684; VDP90091.1; -; Genomic_DNA.
DR   WBParaSite; ECPE_0001285701-mRNA-1; ECPE_0001285701-mRNA-1; ECPE_0001285701.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; 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; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000272942}.
FT   DOMAIN          313..481
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   REGION          504..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..525
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58982 MW;  78411FAF67DE57C6 CRC64;
     MTLGTCDCPY FARIELLADK LAQNLPHFNV TKVVKQPHEW KDFTEWIAKE HGWDVTKSPV
     VWRELLDQGG PGTLIGGSNE FQEYVAAYYN EYSSMTTKEM CDVANDNTTF KTAEEAEKRE
     AEDKRVPPST ILIIGAGSPP CTHLLPYLAI HGLFSPNEYI QLDLYDDSNL EHVSYVVETL
     QDTPCKMLVX DLVPSLKVAK QIIILDVVPR IKLSCEDSTI LHNKTSESEV KSLEPRDQWL
     RRRYSFFTSI GLLAQTHCPS NVRILVTGNP GLDTSSMKIA SPINFDVAVL HKAASPRIST
     RQIVGLVGPL VQRVKASVAN NLHVSTHDIV DVIIWGNVGG RTHIDLSKSR VYRRRGADVG
     LTAGPWYSMP TTDAFRDLEW PSEEMARDVF EDRSAFVPRY RGLSHAQSII TFLRGWWTGD
     FTTKDQIISL VVASEEWYGI PKGVVFSFPV IPSSTSSWTV AEDVEISQSI AKELEACVKD
     VLEDWAVVDP NPLEIFLESK KVPTKPEEEI SQAEEEEEEE EFPSK
//