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Database: UniProt
Entry: A0A093NXJ1_PYGAD
LinkDB: A0A093NXJ1_PYGAD
Original site: A0A093NXJ1_PYGAD 
ID   A0A093NXJ1_PYGAD        Unreviewed;       543 AA.
AC   A0A093NXJ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
DE   Flags: Fragment;
GN   ORFNames=AS28_14387 {ECO:0000313|EMBL:KFW66680.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW66680.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW66680.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW66680.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL225030; KFW66680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093NXJ1; -.
DR   STRING; 9238.A0A093NXJ1; -.
DR   Proteomes; UP000054081; 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   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   3: Inferred from homology;
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:UP000054081}.
FT   DOMAIN          53..234
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          244..496
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        76
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         220
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         243
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW66680.1"
FT   NON_TER         543
FT                   /evidence="ECO:0000313|EMBL:KFW66680.1"
SQ   SEQUENCE   543 AA;  60366 MW;  A43487F64FB4853E CRC64;
     GMAFTLEERL QLGIHGLLPP CFLSQDVQVL RVMKNYENKS NDLDKYIVLM TLQDRNEKLF
     YRVLTSDIER FMPIVYTPTV GLACQQYGLA FRRPRGLFIT IHDKGHIATM LNSWPEENIK
     AIVVTDGERI LGLGDLGSYG MGIPVGKLAL YTACGGVHPQ QCLPVLLDVG TDNEALLSDP
     LYIGLKHKRV RGKQYDELID EFMQAVTNKY GMNCLIQFED FANANAFRLL NKYRNRYCTF
     NDDIQGTASV AVAGIFAALR ITKNKLSDHK FVFQGAGEAA MGIAHLILMA MEKEGISRED
     AIKKIWMVDS KGLIVKGRSH LNHEKEMFAQ DHPSVSTLEE VVQKVKPTAI IGVAAVAGAF
     TEKILKDMAA FNERPIVFAL SNPTSKAECT AEQCYRLTEG RGIFASGSPF SKVTLPNGQT
     FFPGQGNNAY VFPGVALGVI ACGVRHISDD IFLITAESIA AEVTEQNLAE GRLYPPLDSI
     REVSLKIAVK IVDWAYKHGL ASWYPEPADK EAFVKRLVYS PDYDSFVIDD YRWPPAAMQT
     QDV
//
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