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Database: UniProt
Entry: A0A2D0T7A7_ICTPU
LinkDB: A0A2D0T7A7_ICTPU
Original site: A0A2D0T7A7_ICTPU 
ID   A0A2D0T7A7_ICTPU        Unreviewed;       596 AA.
AC   A0A2D0T7A7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   Name=me1 {ECO:0000313|RefSeq:XP_017350773.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017350773.1};
RN   [1] {ECO:0000313|RefSeq:XP_017350773.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017350773.1};
RG   RefSeq;
RL   Submitted (SEP-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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR   RefSeq; XP_017350773.1; XM_017495284.2.
DR   AlphaFoldDB; A0A2D0T7A7; -.
DR   STRING; 7998.ENSIPUP00000001451; -.
DR   Ensembl; ENSIPUT00000001524; ENSIPUP00000001451; ENSIPUG00000001029.
DR   GeneID; 108280372; -.
DR   KEGG; ipu:108280372; -.
DR   CTD; 4199; -.
DR   OMA; DRYVFLI; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000221080; Chromosome 20.
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:SF17; NADP-DEPENDENT MALIC ENZYME; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426}.
FT   DOMAIN          104..285
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          295..547
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         270
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         271
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         294
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         478
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   596 AA;  66993 MW;  404DE04AB5027385 CRC64;
     MARRLVARES GEWESMMMMK KMKDGAEEKC STAVATKKRG YDITRNPHLN KGMAFSLEER
     LQLGIHGLLP PCFLSQDVQL LRVLRNYDLK KDDLDRYVLL MGLQDRNEKL FYRVLLCDIE
     RFLPIVYTPT VGLACQQYGL TFRRPRGLFI TIHDRSHIAT LLQSWPETDV RAVVVTDGER
     ILGLGDLGCY GMGIPVGKLA LYTACGGIPP QKCLPIMLDV GTDNEELLKD PLYIGLRHKR
     VRGEAYDELL EEFMKAVTDR YGRNCLIQFE DFANVNAFRL LHKYRNQYLT FNDDIQGTAA
     VAVAGLLAAL HITKSRMSDH TIVFQGAGEA AMGIAELIIM AMEKEGLPHA ECVRKIWMVD
     SKGLIVKGRD HLTPEKQRFA HEHARMKSLE EVVEKLKPTA IIGVAAIAGA FTERIIKNMA
     TFNERPIIFA LSNPTSKAEC TAEQCYTLTQ GRGIFASGSP FDPVTLADGR RFFPGQGNNA
     YVFPGVALGA VSCSMSHIPE QIFLITAETI AGMVTEKDLA EGRLYPPLTC IRDVSFKIAV
     KTVEYAYKHQ MAMLQPEPAD KEALVRSHIY NTDYDDFTVD SYRWPEEAMN IQTCRL
//
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