ID A0A3G8YIG8_9DEIO Unreviewed; 578 AA.
AC A0A3G8YIG8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:AZI44773.1};
GN ORFNames=EHF33_17945 {ECO:0000313|EMBL:AZI44773.1};
OS Deinococcus psychrotolerans.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AZI44773.1,
OG ECO:0000313|Proteomes:UP000276417}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI44773.1, ECO:0000313|Proteomes:UP000276417};
RN [1] {ECO:0000313|EMBL:AZI44773.1, ECO:0000313|Proteomes:UP000276417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-83T {ECO:0000313|EMBL:AZI44773.1,
RC ECO:0000313|Proteomes:UP000276417};
RC PLASMID=unnamed1 {ECO:0000313|EMBL:AZI44773.1,
RC ECO:0000313|Proteomes:UP000276417};
RA Tian J.;
RT "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT of Antarctica.";
RL Submitted (NOV-2018) 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:RU003427}.
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DR EMBL; CP034185; AZI44773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8YIG8; -.
DR KEGG; dph:EHF33_17945; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000276417; Plasmid unnamed1.
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 GO; GO:0008152; P:metabolic process; IEA:UniProt.
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:SF32; NAD-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}; Plasmid {ECO:0000313|EMBL:AZI44773.1}.
FT DOMAIN 95..275
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 285..541
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 260
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 284
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 578 AA; 62983 MW; E3670F35F09B6A97 CRC64;
MTHNLNTPLT THYDVRRDEA GHRYLHPLVL GFDLTRIPLL NKGTAFTSEE RQTLGLDGLL
APQVDSLDDL VTRLYADYTK LQDPLEKHVF LRGVQDRNEV LFYALLSRHV EEMLPIVYTP
TVGLAVQKFS QIYRVPRGLT LSTLNIERAE QALANVPLND VRIIVATDSS AILGIGDQGF
GGMAISIGKL SLYTVAGGVG PDKTLPVELD VGTGRQDLID DPSYLGVKHK RLTGEEYLRF
VDRFVEATLE RYPKAIIQWE DFSRDAAFTV LERYRKVVPS FNDDIQGTGA VVLSGVLNAC
RIKGERLRDQ KIVLSGAGAG GIGVTDALRR GLIRDGLSDA EARARLFVLD SGGLLLSDRK
LDEYKRAYAH DPATLGFEYE GKAPDLLATV KGAGATVLIG LSGIAGTFSE EVVKATLANT
PRPLVFPLSN PTANCEALPS DVLNWTDGAA IVATGSPFDP VELNGQTYPV GQGNNAFIFP
GLGFGCILAR VREITDEMVL EAAYALAAYT ERHYPERIYP PVSELSAASI EVAAAVIKQA
LKDGVAAEFG VRDLSDEALL ERVRGKFWVP KYLPFKLG
//
