ID A0A226DYW3_FOLCA Unreviewed; 658 AA.
AC A0A226DYW3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=Fcan01_14152 {ECO:0000313|EMBL:OXA50632.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA50632.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA50632.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA50632.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA50632.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-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:OXA50632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNIX01000008; OXA50632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226DYW3; -.
DR STRING; 158441.A0A226DYW3; -.
DR OMA; PRCFTTA; -.
DR Proteomes; UP000198287; 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 Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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:UP000198287};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..376
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 386..611
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 658 AA; 74036 MW; 9188913487EEEADD CRC64;
MESEYYLDDK WFWIACVALV CLWALVMYLL CKWAGSCSSK SAGDVGAGGD HVHICTCRKE
CGDPTSASNH KWGTISRSEL LEEILINNNN FGKNGTNARV LFKMDPRRDR LGQRPLHHDA
GDNVCPNMVR GIDYLRDPRL NKGMAFTLEE RQRLGIHGLL PPRFKSQEEQ VRLCKENVAR
YSEDLNKHIY LVGLQDRNER LFYRLISENV QEMLPLVYTP TVGLACQKFG LIFRRPRGLF
ISIHDKGHVY EVLKNWPEND VRAVVVTDGE RILGLGDLGA YGMGIPVGKL SLYTALAGIP
PNYCLPILLD VGTNTQSLLD DPYYIGLNHK RITGPEYDEF IDEFMQAVVR KYGQNTLIQF
EDFANQNAHR LLDKYRNKYC TFNDDIQGTA SVVLAGVLAS LKISKMKLIE HKFLFLGAGE
AACGIADLIY QQMLKEGATS EQAASRIFLC NKNGLLSKNN PTETYTEEKI LFLKDMPHMT
NFAEMVEAIK PTAIFGAAAA KNAFTPAILN RMAELNERPI IFALSNPTSK AECTAEEAYD
HTDGRAIFAS GSPFPIYDKN GRHFEPGQGN NAELANLVSE SDLKVGRLYP PLDDIKAVSM
KIATKIVEDA YKNGYASTYP EPEDKLQFML RGLYDYQNRQ SIPSVWEWSK EVVASRTK
//
