ID A0A0N1AJ29_9PROT Unreviewed; 772 AA.
AC A0A0N1AJ29;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KPF52354.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KPF52354.1};
GN ORFNames=D621_11770 {ECO:0000313|EMBL:KPF52354.1};
OS beta proteobacterium AAP51.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523421 {ECO:0000313|EMBL:KPF52354.1, ECO:0000313|Proteomes:UP000037990};
RN [1] {ECO:0000313|EMBL:KPF52354.1, ECO:0000313|Proteomes:UP000037990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP51 {ECO:0000313|EMBL:KPF52354.1,
RC ECO:0000313|Proteomes:UP000037990};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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:KPF52354.1}.
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DR EMBL; LJHT01000042; KPF52354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1AJ29; -.
DR PATRIC; fig|1523421.3.peg.2609; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000037990; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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; 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; 2.
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.
PE 3: Inferred from homology;
KW Metal-binding {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:KPF52354.1}.
FT DOMAIN 25..158
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 170..411
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 83..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 298
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 772 AA; 83003 MW; 42799556A091F395 CRC64;
MAKKLSDAES LLRDAALEYH RAPTRGKISV TPTKPLSNQR DLSLAYSPGV AYACLAIEEN
PALAHEYTSR GNLVGVVTNG TAVLGLGDIG PLAGKPVMEG KGCLFKKFAG IDVFDLELAE
RDPDKLIDII AALEPTLGGV NLEDIKAPEC FYIEKKLRER MNIPVFHDDQ HGTAIISSAA
LLNGLELVGK HIGEIKVAVS GAGAAAIACL DVMVGLGVKR EHIYVCDSKG LIQSERDDVR
AGKLDESKQR YCQKTSARTL ADVVKGADVF LGCSAAGVLG VEMVMSMARQ PIILALANPE
PEIRPELAKA ARPDCIIATG RSDYPNQVNN VLCFPYIFRG ALDCGATKIT EAMKLACVRE
IAALAKAEAS DEVAAAYQGK ELKFGPDYLI PTPFDVRLIL RIAPAVARAA AESGVAKRPI
HDLEAYRQGL ERFVYQTGMF MRPVFAAAQA RQAQGGARVV YAEGEDERVL RALQVVKEEG
LAQPILVGRP EVVKMRIERA GLRLQAGRDF EICDPENDPR FREYWEAYRG LMARDGVTPE
VAKAAVRRSN TLISALMLRR GEADAMVCGL VGRYDSHLEH VRAVIGRKPG AHTMAAMNAL
MLEDRTLFIT DTFVNEEPSA EELADIALMA AAEVQRFGVP PKVAFLSHSI FGSSSRPSAQ
RMRQAHALFR ERAPAGVESD GEMQGDAALS ESVRRGYLPE TTLSGSANLL VLPNLDAANI
LFNVLKMTGG QGVTVGPILL GAAKPVHILT PSATVRRIVN MTALAVADAA AG
//
