ID A0A0J1GAV7_9BURK Unreviewed; 747 AA.
AC A0A0J1GAV7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KLU36006.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KLU36006.1};
GN ORFNames=AB595_14895 {ECO:0000313|EMBL:KLU36006.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU36006.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-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:KLU36006.1}.
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DR EMBL; LELH02000017; KLU36006.1; -; Genomic_DNA.
DR RefSeq; WP_047825752.1; NZ_LELH02000017.1.
DR AlphaFoldDB; A0A0J1GAV7; -.
DR PATRIC; fig|1406431.3.peg.1962; -.
DR Proteomes; UP000036336; 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; -; 2.
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; 2.
DR PIRSF; PIRSF036684; ME_PTA; 2.
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:KLU36006.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036336}.
FT DOMAIN 33..166
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 178..415
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 91..98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 302
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 747 AA; 78801 MW; 7FE6D87938BB3D99 CRC64;
MSTESSLDSG IQEPGKDAQL RADALDYHRS PVRGKIEVVA TKPLSNQRDL SLAYSPGVAY
ACEEIAANPA MAAEYTSRGN LVAVISNGTA VLGLGNIGPL ASKPVMEGKG CLFKKFAGVD
VFDLELAEND PDKLIEAIAM LEPTVGGINL EDIKAPECFY IEKKLSERMN IPVFHDDQHG
TAIISSAALL NALKVVGKDI GAVKLVASGA GAAAIACLDM MVSLGVRQQN IYVTDSRGVI
WKGREANMEA NKARYAQDTS ARSLADIVDG ADVFLGCSTA GVLTADMVRT MAARPVILAL
ANPEPEIRPE VAKAARPDCI VATGRSDYPN QVNNVLCFPY IFRGALDCGA TRITTEMKLA
CVTAIAELAE AEANDAVAAA YAGQDLSFGP DYIIPKPFDP RLMAAIAPAV AAAAQASGVA
TRPIEDMGAY REQLAALTYH TSFFMRPVFA KARALNASDL RRVAYAEGAD PRVLRAVQTV
VDEGLGKPVL IGRGAEIEQA IRQSGLRLRR DADYTLAECG DDTTARGTAM LAAGEVDALI
CGMKGSYDSH LAHVQRDIGL APGAEVMAAM NALVLDKGTL FITDTYVNDQ PSGKELAAIT
RLASDELRQF GLDPKVALVS HSIFGSSQRP SAQRMREARE ILAKEAPELA VLGEVHGDAA
LDENIRAVYL PAGQNSFEGS ANLLVMPSLD AANILFNVLK VSSGKGVTVG PILLGAAKSV
HILSPSATVR RIVNMTALAV ADVKADA
//
