ID   A0A0V1A8A7_9BILA        Unreviewed;      1296 AA.
AC   A0A0V1A8A7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   Name=Me3 {ECO:0000313|EMBL:KRY21083.1};
GN   ORFNames=T12_6975 {ECO:0000313|EMBL:KRY21083.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY21083.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY21083.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY21083.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:KRY21083.1}.
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DR   EMBL; JYDQ01000019; KRY21083.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; 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:UP000054783}.
FT   DOMAIN          805..988
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          998..1257
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          387..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1296 AA;  145567 MW;  0D7FB26978B60C1C CRC64;
     MKLHRTFYCQ NFYFCNFINL VHMADCDSSS ASADNESLVT RLNFTAKSVL VYSINAAYES
     QPVKSRLDWK HVTVPSEADT FISNDQEKAG DVNEASSNSA IRESRSLKWN LRSSCYESCS
     RQRSFTWNEV IASNAYHLQS RPSEMNSPKQ QKAGNAISSG AFSKLPKLHL KIRRKPVIQQ
     SEVDSRICNV INSFDDDQQA ATATFANTTH ADVENLTVEN ESRRKLRWKL RSATRREVCI
     CWANKFQVID VSSKPELQRC DNANLSDCAT MSCNDPFDQP LCKECFLSSY GNEQLDNDWM
     NAEVNYCDFP TSLGEQRNQI NRNTNQLEIA IEDYEDNFAD TFKNLPALHT PNPALSEPDV
     NDFELAEEET YQAFIANLRL LTQSENAVDG DKDTNAPIQR EEEKELHEDG NASSLPVEMF
     NTVDNTDVLF NESSSNDTVV ENVQIVNETV NCREEVEVVA QSAACSEAKK AKRTTRCRKA
     KPCTAADKAT GSKRKYCKRS DRSTGEVATT STTGNNCYSQ MLVTLQPQQQ QQPYQFVIQQ
     NNQILNQILL VPVVVQNSAP MVVQQPSTNS NSNSNANAQQ VKYLDDNIID QMESGFCRRK
     PRLILKRRPE AMQPRNVHHK NDVTTQPAVS SLVTLSAAVV VVVVVGGHLH FQLQQTSFSV
     FAFHFTTRLL FSHSSFRRLT KKNEPRGVQL CKANDVVALD WPNGGAISTQ PHQRQAQLPV
     YRLPCPRLGG AAQSTDQQSR QFSILFQRLF RGGIAFTIKE RHILGIHGLL PPNVLTAEQQ
     VQRILKNLDN ESSDLRRYVA LNDLQDRNEK LFYRVLCENV EKYMPIVYTP TVGLACQKFG
     LIFRRPKGIF ISIQDDSVER IYNILAAWPE KDIRAICVTD GERILGLGDL GAYGMGIPVG
     KLSLYVALAG VHPQWCLPVV LDVGTDNEEI KKDPFYIGMK HERIRDERYD RLVDNFLRAA
     VERFGPTCLI QFEDFANQNA FRFLDKYKKA YCTFNDDIQG TASVAVAGLI SAAKMTKKSL
     KDHRVLFYGA GEAAVGIAKL TCLAMSNEGI PFEEAKKNIW MVDSKGLIVK GRSHLNEHKL
     EFAQDHAEVQ SLEDIINKVK PTAIIVIWML DFAGAATITG AFNETILRTM AKLNDRPIIF
     ALSNPTSKSE CTAEQAYKFT DGRAIFASGS PFDKVEYGGK VFCPGQGNNS YIFPGVALGA
     ICSMARHIPD EVFLIAAQVL SNLVTEKHME EGRVYPPLNV VREISVKIAA AVAEQCYKSG
     EAACFPKPDD MEAFIRSKVY SYEYDSYVPD MYEFEH
//