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Database: UniProt
Entry: A0A2K5NPQ5_CERAT
LinkDB: A0A2K5NPQ5_CERAT
Original site: A0A2K5NPQ5_CERAT 
ID   A0A2K5NPQ5_CERAT        Unreviewed;       487 AA.
AC   A0A2K5NPQ5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Malic enzyme NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000039311.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000039311.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   AlphaFoldDB; A0A2K5NPQ5; -.
DR   STRING; 9531.ENSCATP00000039311; -.
DR   Ensembl; ENSCATT00000063622.1; ENSCATP00000039311.1; ENSCATG00000042284.1.
DR   GeneTree; ENSGT00950000183134; -.
DR   OMA; PHKVAFA; -.
DR   Proteomes; UP000233060; Unplaced.
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; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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:SF27; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 3.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT   DOMAIN          88..219
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          221..438
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   BINDING         206
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         207
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   487 AA;  55622 MW;  42A608FDF4DA7B3E CRC64;
     HLSRQIVSTT CTLACRHLHI KEKGKPFMLN PRTNKGMAFT LQERQMLGLQ GLLPPKIQTQ
     DIQALGFHRN LKKMTSPLET YIYIMEIQER NEKLFYRILQ DDTESLMPIV YTPTVGLVCS
     QYGHIFRRPK GLFMSISDRA HIRSIVDKCI PVCIDVGTDN IALLKDTFYI GLYQKQDRTQ
     QYDDLIDEFM KAITDRYGWN TLIQFEDFGN HNAFRRDYSW NCKSQKSMSM VENGLSEEEA
     QKKIWMFDKY GLLVKGQKAK IDSHQEPFTY PVPESIPDTF EDVVNTMRTS TTIGVAGAGH
     LFTPDVIRAM TPINERPVIF TLSNPIAQAE CTAEEAYTLT EGKCLFASGS PFGPVKLTDG
     RIFTPDQGNN VYIFPGVSLA VILCNTQHIS DNVFLEAAKA LTSQMRDEKL AQGRLYPPLA
     NIQKVSINIA IKVIEYLYAN KMAFQYPEPE DKAKYVKERI WRSEYDSLLP DVYEWLEPAS
     SPPVITE
//
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