ID   A0A0V1LHT1_9BILA        Unreviewed;      1204 AA.
AC   A0A0V1LHT1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   Name=ME1 {ECO:0000313|EMBL:KRZ59027.1};
GN   ORFNames=T02_9061 {ECO:0000313|EMBL:KRZ59027.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ59027.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ59027.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ59027.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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:KRZ59027.1}.
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DR   EMBL; JYDW01000048; KRZ59027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1LHT1; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; 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   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003426};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT   DOMAIN          722..905
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          915..1165
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          366..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ59027.1"
SQ   SEQUENCE   1204 AA;  135948 MW;  187632F0787B33C6 CRC64;
     LKSVLDFVNL VHMAGCDSSS ASADNESLVT RLNFTAKSVL VYSINAAYES QPVKSRLDWK
     HVTVPSEADT FISNDQEKAG DVNEASSNSA IREPRSLKWN LRSSCYKSCS RQRSFTWNEV
     FASNAYHLQS RPSEMNSPKQ QKAGNAISSG AFSKLPKLHL KIRRKPVIQQ SEVDSRICNV
     INSFDDDQQA ATATFANTKH ADVENLTVEN ESRRKLRWKL RSATRREDVS SKPELQRCDN
     ANLSDCATMS YNDPFDQPLC KECFLSSYGN EQLDSDWMNA EENYCDFPTS LGEQRNQINR
     NTNQLEIAIE DYEDNFADTF KNLPALHTPN PALSEPDVND FELAEEETYQ AFIANLRLLT
     QSENAVDRDK DTNAPIQREK EKELHEDGNA SSLPVEMFNT VDNTDVLFNE SSSNDTVVEN
     VQIVNETVNC REEEEVEVVA QSAACSEAKK AKRTTRCRKA KPCTAADKAT GSKRKYCKRS
     DRSTGEVATT STTGNHCYSQ MLVTLQPQQQ QQQQQPYQFV IQQNNQILNQ ILLVPVVVQN
     SAPMVVQQPS TNLNSNTNAQ KVKYVDDNII DQMESGFCRH KPRLILKRRP EAMQPRNLQQ
     TSFSAFAFHF TTRLLFSHSS FRRLTTLWRW TGRMAAPFQP NRTSVKHNSQ YTDCRVRGWE
     VLHNPRTNKG IAFTIKERHI LGIHGLLPPN VLTAEQQVQR ILKNLDNESS DLRRYVALND
     LQDRNEKLFY RVLCENVEKY MPIVYTPTVG LACQKFGLIF RRPKGIFISI QDDSVERIYN
     ILAAWPEKDI RAICVTDGER ILGLGDLGAY GMGIPVGKLS LYVALAGVHP QWCLPVVLDV
     GTDNEEIKKD PFYIGMKHKR IRDERYDRLV DNFLRAAVER FGPTCLIQFE DFANQNAFRF
     MDKYKKAYCT FNDDIQGTAS VAVAGLISAA KMTKKSLKDH RVLFYGAGEA AVGIAKLTCL
     AMSNEGIPFE EAKKNIWMGR SHLNEHKLEF AQDHAEVQSL EDIINKVKPT AIIVIWILDF
     AGAATITGAF NETILRTMAK LNDRPIIFAL SNPTSKSECT AEQAYKFTDG RAIFASGSPF
     DKVEYGGKVF CPGQGNNSYI FPGVALGVIC SMARHIPDEV FLIAAQVLSN LVTEKHMEEG
     RVYPPLNVVR EISVKIAAAV AEQCYKSGEA ACFPKPDDME AFIRSKVYSY EYDSYVPDMY
     EFEH
//