ID U5EW70_9DIPT Unreviewed; 648 AA.
AC U5EW70;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
OS Corethrella appendiculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Chaoboridae;
OC Corethrella.
OX NCBI_TaxID=1370023 {ECO:0000313|EMBL:JAB58310.1};
RN [1] {ECO:0000313|EMBL:JAB58310.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAB58310.1};
RA Ribeiro J.M.C., Chagas A.C., Pham V.M., Lounibos L.P., Calvo E.;
RT "An insight into the sialome of the frog biting fly, Corethrella
RT appendiculata.";
RL Insect Biochem. Mol. Biol. 44:23-32(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
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}.
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DR EMBL; GANO01001561; JAB58310.1; -; mRNA.
DR AlphaFoldDB; U5EW70; -.
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:SF80; GH17657P-RELATED; 1.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426}.
FT DOMAIN 164..345
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 355..608
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 21..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 330
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 331
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 354
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 495
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 539
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 648 AA; 72129 MW; FD2D2D68E8C27F18 CRC64;
MSTKIAQFSY EKFIKDGVYS TEQHQQQNGS SSDQLNNKNK LNIRTVDSEL SKQKDRKRFL
FGNFKSDDSN KNNMSDNNCR DRLGQWSSGS DSEAPCLVSG NDRLRTGRLN KGLAFTLEER
QALGIHGFLP AVTRTQEEQV QHCIQLLARY ENDLDKYIYL MGLLDRNERL FYRTVSSDIV
NMMPLIYTPV VGLACQKYSL IYQQPKGMFI TINDKGHVYD LLKNWPENDV RAICVTDGER
ILGLGDLGAN GMGIPVGKLA LYTALAGIKP HQCLPVTLDV GTNTQSILDD PLYIGLKHKR
VTGQVYDDFV DEFMKAAVRR FGQNCLIQFE DFGNSNAFRF LDKYRNNYCT FNDDIQGTAS
VALSGVFASL RITKTSLSEN KIVFQGAGEA ALGIAGLIVM AMMAEGMTQE EARKRIWMVD
SKGLIVKDRP KGGISGHKHD FAHEHEPIDS LADVVKQLKP TVLIGAAAIA KAFTPEILKT
MADNNERPVI FALSNPTSKA ECTAEEAYTH TDGKAVFASG SPFPPFTYKG KTFHPGQGNN
SYIFPGIALG VICAAVKKIP EDVFLISAKR LAELVTEADL EQGSLYPPLE TIQLCSLKIA
AKVMDYAYET GIASYFPEPQ NKEEFIQSQM YNTNYKSAIQ NVYAWPKL
//
