ID Q5U525_XENLA Unreviewed; 613 AA.
AC Q5U525;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=me3.L {ECO:0000313|RefSeq:NP_001088519.1,
GN ECO:0000313|Xenbase:XB-GENE-973123};
GN Synonyms=LOC495390 {ECO:0000313|EMBL:AAH84860.1}, me3
GN {ECO:0000313|RefSeq:NP_001088519.1,
GN ECO:0000313|Xenbase:XB-GENE-973123};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH84860.1};
RN [1] {ECO:0000313|RefSeq:NP_001088519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH84860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole {ECO:0000313|EMBL:AAH84860.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001088519.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; BC084860; AAH84860.1; -; mRNA.
DR RefSeq; NP_001088519.1; NM_001095050.1.
DR GeneID; 495390; -.
DR KEGG; xla:495390; -.
DR AGR; Xenbase:XB-GENE-973123; -.
DR CTD; 495390; -.
DR Xenbase; XB-GENE-973123; me3.L.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 495390; Expressed in intestine and 20 other cell types or tissues.
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:SF20; NADP-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT DOMAIN 123..304
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 314..566
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 313
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 497
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 613 AA; 67477 MW; 2BD0705831EF1F82 CRC64;
MNSVIGKQAV SLGIRAASGA PRLGLWAPVL SHPQSLIRVC HTAAGGGHPA KSQAIKKRGY
DITRNPYLNK GMAFTLEERL QLGIHGLLPP CFLSQDVQVL RVMKSYETKS SDLDKYIILM
TLQDRNEKLF YRVLTSDIER FMPIVYTPTV GLACQQYGLA FRRPRGLFIT IHDKGHIATM
LNSWPEEDIK AIVVTDGERI LGLGDLGGYG MGIPVGKLAL YTACGGVHPQ QCLPVLLDVG
TDNEALLNDP LYIGLKHKRV RGKEYDELID EFMQAVSNKY GMNCLIQFED FANSNAFRLL
NKYRNKYCTF NDDIQGTASV AVAGILAALR ITNNKLSDHK FVFQGAGEAA MGIATLITMA
MEKEGTSRGD AIKKIWMVDS KGLIVKGRGN LNHEKEVFAQ DHPQVKTLEE AVQILKPTAI
IGVAAISGAF TEKIIKDMAA FNERPIIFAL SNPTSKAECT AEQCYQLTEG RGIFASGSPF
SKVTLANGQT FYPGQGNNAY VFPGVALGVI ACGVRHISED LFLTTAEMIA EMVTAENLAE
GRLYPPLSSI RDVSFKIAVK IVDYAYKNNM ASWYPEPADK ESFVRSLIYS PDYDSSTIDS
YHWPTKAMEI QDV
//
