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Database: UniProt
Entry: S8C9K9_9LAMI
LinkDB: S8C9K9_9LAMI
Original site: S8C9K9_9LAMI 
ID   S8C9K9_9LAMI            Unreviewed;       439 AA.
AC   S8C9K9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   23-MAY-2018, entry version 21.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
DE   Flags: Fragment;
GN   ORFNames=M569_11164 {ECO:0000313|EMBL:EPS63619.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS63619.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS63619.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A.,
RA   Kondrashov A.S., Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a
RT   low number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|RuleBase:RU003426}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPS63619.1}.
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DR   EMBL; AUSU01005362; EPS63619.1; -; Genomic_DNA.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   Gene3D; 3.40.50.10380; -; 1.
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   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; SSF51735; SSF51735; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000015453};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003426};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT   DOMAIN      117    298       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      308    438       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE    140    140       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    211    211       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       283    283       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       284    284       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       307    307       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EPS63619.1}.
FT   NON_TER     439    439       {ECO:0000313|EMBL:EPS63619.1}.
SQ   SEQUENCE   439 AA;  48720 MW;  E8BE193A33F7762C CRC64;
     RMESFLKNHR GGESVLDLSP RSTVGGGVED VYCEDRASED QLVTPWTISV ASGYSMLRDP
     KHNKGLAFTE KERDAHYLRG LLPPAIISQE LQEKRLMQNI RDYEVPLHKY ISLMELAERN
     ERLFYKLLID NVEELLPVVY TPTVGEACQK YGSIFRRPQG LYISLKEKGK ILEVLRNWPE
     RGIQVIVVTD GERILGLGDL GCQGMGIPVG KLSLYTALGG IRPSACLPIT IDVGTNNAKL
     LNDEFYIGLK QKRATGEEYY SFLHEFMTAV KQNYGEKVLI QFEDFANHNA FELLAKYGTT
     HLVFNDDIQG TASVVLSGLI ASLKLLGGTL ADHTFLFLGA GEAGTGIAEL IALEISKKTN
     VPVEETRKKI WLVDSKGLIV SSRKESLQHF KKPWAHEHEP VGNLLDAVKA IKPTALIGTS
     GVGKTFTKEV VQAMAAFNE
//
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