ID A0A257EI71_9BURK Unreviewed; 766 AA.
AC A0A257EI71;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:OYU13612.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:OYU13612.1};
GN ORFNames=CFE38_00945 {ECO:0000313|EMBL:OYU13612.1};
OS Comamonadaceae bacterium PBBC1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=2015580 {ECO:0000313|EMBL:OYU13612.1, ECO:0000313|Proteomes:UP000216161};
RN [1] {ECO:0000313|EMBL:OYU13612.1, ECO:0000313|Proteomes:UP000216161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBBC1 {ECO:0000313|EMBL:OYU13612.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU13612.1}.
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DR EMBL; NKIP01000001; OYU13612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EI71; -.
DR Proteomes; UP000216161; 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; 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.
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:OYU13612.1}.
FT DOMAIN 26..159
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 171..408
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 84..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 295
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 766 AA; 82048 MW; 10275616894996C7 CRC64;
MSQKPLSPAE EALRDAARDY HRFPTRGKVS VNPTKPLSNQ RDLSLAYSPG VAYPCLDIEA
DPSKAAEYTS RGNLVAVITN GTAVLGLGDI GPLAAKPVME GKGCLFKKFA GIDVFDIELA
ERDPDKLVDI IAAMEPTLGG INLEDIKAPE CFYIEKKLRE RMNIPVFHDD QHGTAIIASA
AMLNGLELVG KDIGSIKLAV SGAGAASIAC LDVMVGLGVK IENIFVCDSK GVIYEGRPGG
YDESKARYAQ KTEARSLADA VNGADVFLGC SAPGVMTVDM IKTMARDPVI LALANPEPEI
RPELAKAARP DCIIATGRSD YPNQVNNVLC FPYIFRGALD CGATKITEAM KLACVRQIAD
LAKADISEEV ASAYAGKELS FGRDYLIPTP FDSRLILRIA PAVAQAAADS GVATRPITDM
DAYRQQLQSF VTQTGILMRP IFNAAKAVPQ DAKRVAYADG EDERALRAAQ MAIDEKVAHP
ILIGRPGVIA ARIEKAGLRM RLGVDVDNVN PEDDARFRQY WEHYHQLMKR NGATPAVAKA
AVRRSNTIIG ALMVSLGDAD GLICGLTGSY MTHLERIESI LGKRAGVTNY AAVNALMSDL
GPLFITDTYV NEDPSAEQLA EIAYMAAQEV QRFGIVPKVA FLSHSSYGSS KRASARKMRL
ARDLFVAQHP DIECDGELHG DAALQPEIRN VYLEDSTLSG SANLLVCPNL DAANILYNVM
KTTTSGGVTV GPVLMGAAGT AHILTPAATV RRVLNMTALA VAQAHH
//
