ID   A0A0V0SKZ2_9BILA        Unreviewed;      1248 AA.
AC   A0A0V0SKZ2;
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:KRX27551.1};
GN   ORFNames=T07_13938 {ECO:0000313|EMBL:KRX27551.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27551.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX27551.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX27551.1};
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:KRX27551.1}.
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DR   EMBL; JYDL01000003; KRX27551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SKZ2; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003426};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        608..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        633..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          765..948
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          958..1209
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          375..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1248 AA;  140572 MW;  50CE0B8C608026A1 CRC64;
     MKLHRTFYCQ NFYFCNFINL VHMAGCDSSS ASADNESLVT RLNFTAKSVL VYSINAAYES
     QPVKSRLDRK HVTVPSEADT FISNDQEKAG DVNEASSNSA IREPRSLKWN LRSSCYESCS
     RQRSFTWNEV IASNAYHLQS RPSEMNSPKQ QKAGNAISSG ALSKLPKLHL KIHRKPVIQQ
     SEVDSRICNV INSFDDDEQA ATATISNTTH ADVENLTVEN ESRRKLRWKL RSATRRQDVS
     SKPELQRCDN ANLSDCATMS CNDFFDQPLC KECFLSSYGN EQLDNDWMNA DVNYCDFPTS
     LGEQRNQINR NTNQLEIAIE DYEDNFADTF KNLPALHTPN PALSEPDVND FELAEEETYQ
     AFIANLRLLT QSENAVDGDK DTNTPIQREE EKELHEDGNA SSLPVEMFNT VDNTDVLFNE
     SSSNDTVVEN VQIVNETVNC REEEEVEVVA QSAACSEAKK AKRTTRCRKA KPCTAADKAT
     GSKRKYCKRS DRSTGEVATT AATTGNNCYS QMLVTLQQQQ QQQQQPYQFV IQQNNQVLNQ
     ILLVPVVVQN SAPMVVQQPI MNSNSNANAQ QVKYLDDNII DQMESGFCRR KPRLILKRRP
     EAILPRNVHR LCLLLLLLLG GIFIFSFNKP ASPLSHFISQ FGCYFLILHF AGLRKKMSLV
     ACNYAKLTML WRWTGRMAAP FQPNRTSVKH NSHYTDCRVR GWEVLHNPRT NKGIAFTIKE
     RHILGIHGLL PPNVLTADQQ MQRILKNLDN ESSDLRRYVA LNDLQDRNEK LFYRVLCENV
     EKYMPIVYTP TVGLACQKFG LIFRRPKGIF ISIQDDSVER IYNILAAWPE KDIRAICVTD
     GERILGLGDL GAYGMGIPVG KLSLYVALAG VHPQWCLPVV LDVGTDNEEI KKDPFYIGMK
     HKRIRDERYD RLVDNFLRAA VERFGPTCLI QFEDFANQNA FRFLDKYKKA YCTFNDDIQG
     TASVAVAGLL SAAKMTKKSL KDHKVLFYGA GEAAVGIAKL TCLAMSNEGI PFEEAKKNIW
     MVDSKGLIVK GRSHLNEHKL EFAQDHAEVQ SLEDIINKVK PTAIIGAATI TGAFNETILR
     TMAKLNDRPI VFALSNPTSK SECTAEQAYK FTDGRAIFAS GSPFDKVEYG GKVFCPGQGN
     NSYIFPGVAL GAICSMARHI PDEVFLIAAQ VLSNLVTEKH MEEGRVYPPL NVVREISVKI
     AAAVAEQCYE SGEAACFPKP DDMEAFIRSK VYSYEYDSYV PDMYEFEH
//