ID A0A3R8NA64_9BURK Unreviewed; 772 AA.
AC A0A3R8NA64;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RRN43934.1};
GN ORFNames=EHV23_11115 {ECO:0000313|EMBL:RRN43934.1};
OS Lautropia dentalis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Lautropia.
OX NCBI_TaxID=2490857 {ECO:0000313|EMBL:RRN43934.1, ECO:0000313|Proteomes:UP000270261};
RN [1] {ECO:0000313|EMBL:RRN43934.1, ECO:0000313|Proteomes:UP000270261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 2505 {ECO:0000313|EMBL:RRN43934.1,
RC ECO:0000313|Proteomes:UP000270261};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Lautropia sp. KCOM 2505 (= ChDC F240).";
RL Submitted (NOV-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:RRN43934.1}.
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DR EMBL; RRUE01000002; RRN43934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8NA64; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000270261; 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}.
FT DOMAIN 25..158
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 170..407
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 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 772 AA; 82516 MW; 2EA5F20A356090C2 CRC64;
MTKQLSAAEA ALRDAAREYH AQPAPGKVSV RPTKPLSNQR DLSLAYSPGV AYPCLDIQAD
PAKAAEYTSR GNLVGVITNG TAVLGLGDIG PLAGKPVMEG KGCLFKKFAG IDVFDIELAE
RDPDKLVEII MALEPTLGGV NLEDIKAPEC FYIERELRQK MKIPVFHDDQ HGTAIISGAA
LVNGLELVGK PIGDVKVAVS GAGAAALACL DIFVALGVNP KNVYVADSKG VIYKGRPGGY
DESKARYAQD TEARTLADVV KGADVFLGCS TSGVLTGEMV KSMGEQPVIL ALANPEPEIR
PEDARAARPD CIIASGRSDY PNQVNNVLCF PYIFRGALDC GASCITEEMK LACVREIAAL
AKAEPSDEVA DAYTGKNLNF GPDYIIPTPF DPRLILRIAP AVAEAAAASG VASRPIEDLD
AYRQSLYHYV YSTGLLMRPV VAAAKAAPAA IKRVAYAEGE DERVLRCAQT AIDEGLAYPI
LIGRPAVIED RILKAGLRMR AGQDMEIVNP DDDARFRQYW EEYWRLMGRR GVSQEAAKAG
VRRATTLIAA LMVRLGDADT MLCGTLGRFD VHLGHIRDVI GSRPGKPLAT LNALTMGNRT
LFITDTYVND SPDAETLAKI AQMAAEEVNN FGIPPKVAFV SHSQFGGSNR PSAIKMREAR
DIFRSVVPNV SCDGEMHGDA ALRPELRDRL VPDSTLEGEA NLLVCPNLDS ANILFNVLKT
TDGHGVTIGP ILLGSAFPVH VMTPSATVRR LVNMTALAVA EVAARKAKCA AA
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