ID A0A2S4MN17_9BURK Unreviewed; 766 AA.
AC A0A2S4MN17;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:POR56152.1};
GN ORFNames=B0G62_101549 {ECO:0000313|EMBL:POR56152.1};
OS Paraburkholderia eburnea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR56152.1, ECO:0000313|Proteomes:UP000237381};
RN [1] {ECO:0000313|EMBL:POR56152.1, ECO:0000313|Proteomes:UP000237381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18070 {ECO:0000313|EMBL:POR56152.1,
RC ECO:0000313|Proteomes:UP000237381};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JAN-2018) 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:POR56152.1}.
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DR EMBL; PQGA01000001; POR56152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4MN17; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000237381; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000237381}.
FT DOMAIN 24..157
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 169..406
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 82..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 293
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 766 AA; 83241 MW; 4CCE97A90D4B5EC1 CRC64;
MSNSNPATNK LREAALDYHE FPTPGKIAIA PTKQMINQRD LSLAYSPGVA FACEAIVENP
LNAARFTARS NLVGVVSNGT AVLGLGNIGP LASKPVMEGK AVLFKKFAGI DVFDIELNET
DPHKLVDVIA ALEPTFGGIN LEDIKAPECF IVEREARKRM KIPVFHDDQH GTAIVVAAAF
TNGLKVVGKD IKQVKLVASG AGAAALACLD LLVDLGLPLE NIYVSDLAGV VYKGRTELMD
PDKERFARET DARTLAEVIE GADIFLGLSA GGVLKQDMVK RMAPKPLILA LANPTPEILP
ELALEVRPDA VLATGRTDYP NQVNNVLCFP FIFRGALDVG ATTITREMEI AAVNAIAELA
RQEQSDVVAT AYGIQDLQFG PEYLIPKPFD PRLIVKIAPA VAKAAMDAGV ATRPIEDMDA
YEQHLQQFVY HSGTTMKPIF QIARAVEPEK KRIVFAEGEE ERILRAVQIV VDENLARPIL
IGRPAVIEQR IARCGLRLVA GQDYTVVNTD HDERYREFWQ SYAKLMARKG ITAQMAKLEM
RRRTTLIGAM LVEKGEADGM ICGTVSTTHR HLHFIDQIIG KKEGCKVYGA MNALVLPNRQ
IFVVDTHVNV DPTPEQLAEI TIMAAEEVRR FGIEPKIALC SHSNFGSSNA PSAQKMRDLL
VILQERAPDL QVDGEMHGDV ALDATLRREV LPESTLEGEA NLLVMPNIDA ANISYNLLKT
AAGNNIAIGP ILLGAAKPVH VLTASATVRR IVNMTALLVA DVNATR
//
