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Database: UniProt
Entry: A0A1J5GYC4_9CYAN
LinkDB: A0A1J5GYC4_9CYAN
Original site: A0A1J5GYC4_9CYAN 
ID   A0A1J5GYC4_9CYAN        Unreviewed;       463 AA.
AC   A0A1J5GYC4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OIP71912.1};
GN   ORFNames=AUK48_11765 {ECO:0000313|EMBL:OIP71912.1};
OS   Oscillatoriales cyanobacterium CG2_30_44_21.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales.
OX   NCBI_TaxID=1805292 {ECO:0000313|EMBL:OIP71912.1, ECO:0000313|Proteomes:UP000185977};
RN   [1] {ECO:0000313|EMBL:OIP71912.1, ECO:0000313|Proteomes:UP000185977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_21 {ECO:0000313|EMBL:OIP71912.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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, ECO:0000256|RuleBase:RU003427}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIP71912.1}.
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DR   EMBL; MNZA01000200; OIP71912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5GYC4; -.
DR   STRING; 1805292.AUK48_11765; -.
DR   Proteomes; UP000185977; Unassembled WGS sequence.
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; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.30.70.260; -; 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; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
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; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR   Pfam; PF13291; ACT_4; 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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427}.
FT   DOMAIN          13..89
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         213
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         238
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   463 AA;  49641 MW;  E21DA688AA1D2A69 CRC64;
     MQQLTPNPSF SLTIRVQLLN RAGMLSSVIR ALAEAGGNLG QIDLIQQTRK ISVRDITVSA
     YSTEHMDQLI AVVKTVPEIR VLDIYDRTFQ VHQGGKIHLE AKIAVKGQDD LAMVYTPGVA
     RVCMAIAEDK RKVYDYTIKC NTIAVITDGT AVLGLGDIGP EAAMPVMEGK AMLFKQFAGL
     DAFPICLNTK DVDEIVETVK RISPTFGGIN LEDISSPRCF EIERRLKAEL DIPVYHDDQH
     GTAIVVVAAA LNAFKVVSKP IDQVRIVMNG AGAAGIAVAR LLREAGVKRI EMCDSRGCIS
     KDRPDLTPEK SEFASDRTGS LADVIKGADM FIGLSVQGAL TPEMVRSMAP APIVFAMANP
     NPEIQPELVE NDVAVIATGR SDYANQINNV LAFPGIFRGA LDARVTTITT QMNLGAAQAI
     ASLVSSSDLA PDFIIPSVFD PRVSHAVAAA VHAVARQQGL ANA
//
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