ID A0A923S0Y0_9BURK Unreviewed; 768 AA.
AC A0A923S0Y0;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:MBC5763715.1};
GN ORFNames=H8R02_04590 {ECO:0000313|EMBL:MBC5763715.1};
OS Ramlibacter albus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=2079448 {ECO:0000313|EMBL:MBC5763715.1, ECO:0000313|Proteomes:UP000596827};
RN [1] {ECO:0000313|EMBL:MBC5763715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GTP1 {ECO:0000313|EMBL:MBC5763715.1};
RA Kang M.;
RT "Ramlibacter sp. GTP1 16S ribosomal RNA gene genome sequencing and
RT assembly.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family.
CC {ECO:0000256|ARBA:ARBA00008756}.
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:MBC5763715.1}.
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DR EMBL; JACORU010000001; MBC5763715.1; -; Genomic_DNA.
DR RefSeq; WP_187080149.1; NZ_JACORU010000001.1.
DR Proteomes; UP000596827; 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 FunFam; 3.40.50.10380:FF:000003; NADP-dependent malic enzyme; 1.
DR FunFam; 3.40.50.720:FF:000095; NADP-dependent malic enzyme; 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; IPR051674; Malate_Decarboxylase.
DR InterPro; IPR032683; Malate_DH.
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 NCBIfam; NF009501; PRK12861.1; 1.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF12434; Malate_DH; 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|ARBA:ARBA00022723,
KW 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:UP000596827}.
FT DOMAIN 27..161
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 173..410
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 85..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 297
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 768 AA; 83101 MW; 61A0D98BF8302A38 CRC64;
MPNEVNTEDK RAELRRAALE YHEQPIPGKV AIAATKQLVN QHDLSLAYSP GVAAPCEEIV
KDPANAFRYT ARGNLVAVIT NGTAVLGLGD IGPLAAKPVM EGKGVLFKKF AGIDVFDIEI
AEKDNLDKLV DIIAALEPTF GGINLEDIKA PDCFYVERKL RERMKIPVFH DDQHGTAICV
AAAIINGLKV VGKDISKVKL VTSGAGAAAL ACVGLLLKLG MPRENIWLTD LAGVVYEGRK
ELMDEDKIQF AKNTPLRKLG DVMEDADVFL GLSAGGVLKP DMVKKMAANP IILALANPNP
EINPEDAKAA RADCIIATGR TDYPNQVNNV LCFPYIFRGA LDSGATTITV EMEIAAVHAI
AELAQAEQSE VVAAAYAGQQ LAFGPDYLIP KPFDPRLMMK IAPAVAKAAA DSGVALRPIP
DMDAYRDKLQ TFVYASGTTM KPIFTAAKTA AKKRVAYCEG EEERVLRAAQ VVVDEAIARP
TLIGRPTIIA ERVEKFGLRL REGVDYDVVN TEYDERYRDF WQTYHRMTDR KGVTAQMAKI
EMRRRLTLIG AMLLHKGQVD GMICGTWGTT DIHLRYLDQV IGKRPGVKTY ACMNGLMLPG
RQIFLVDTHV NYDPTAAQLA EITVMAAEEM LRFGVKPKVA LLSHSNFGSG NTPTAIKMRE
TLALLQAEAP WLEVDGEMHG DVALDGHARN LLMPRSTLAG DANLLVLPNI DAANISYNLL
KTAAGGNIAI GPVLLGAAKP VHILTASTTV RRIVNMTALT VADANAAR
//
