ID A0A1Y5SMZ6_9RHOB Unreviewed; 751 AA.
AC A0A1Y5SMZ6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:SLN43307.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:SLN43307.1};
GN Name=tme {ECO:0000313|EMBL:SLN43307.1};
GN ORFNames=PEL8287_02173 {ECO:0000313|EMBL:SLN43307.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN43307.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN43307.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN43307.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWFL01000005; SLN43307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SMZ6; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000193827; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 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:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SLN43307.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 751 AA; 81209 MW; 7158FC072F52B98A CRC64;
MAKMKITREE ALAFHLEPTP GKFEITATVP MTTQRDLSLA YSPGVAVPCE EIAANPETAY
DYTNKGNLVA VISNGTAVLG LGNLGAVASK PVMEGKAVLF KRFADVNSID IELDTEDPEA
FINAVKLMGP TFGGINLEDI KAPECFIIEQ QLKEIMDIPV FHDDQHGTAV ICAAGLINAL
HISGKKIEDV KIVLNGAGAA GIACIELLKS MGARHDNCIV CDTKGVIYQG RTEGMNQWKS
AHAVKTDLRE LGEAMKDADV FLGVSVKGAV TEDMIASMAD NPVIFAMANP DPEITPEEAH
AVRADAIVAT GRSDYPNQVN NVLGFPYLFR GALDVHARAI NDEMKIACAQ ALASLAREDV
PDEVAMAYGQ KLSFGRDYII PTPFDPRLIY TIPPAVARAC MDTGAARRPI VDMEAYEVSL
KARMDPTASI LRSINARARN AQARMIFAEG DDIRVLRAAV QYQRTGFGKA IVIGRDEDVK
AKLEAAGLGD AVREIEVTNA AKSARLEEYK EFLYQRLQRK GFDRHDVHRL AARDRHVFSA
LMLAHGHGDG LVTGATRKSA HVLQLINHVF DAGAEHGAAG ITALLHKGRI VMIADTLVHE
WPDEEDLANI AERAAGVARH LGLEPRVAFV SFSTFGYPRS ERAEKMHQAP KVLEKRGVDF
EFEGEMTVDV ALNVTAQETY PFQRLSGPAN ILVVPARHSA SISVKLMQEM AGATVIGPIL
SGVDKSIQIC SSNFTANDIL NMAVLAACKV G
//