ID A0A011Q0A8_9PROT Unreviewed; 766 AA.
AC A0A011Q0A8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:EXI93166.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EXI93166.1};
GN Name=maeB_1 {ECO:0000313|EMBL:EXI93166.1};
GN ORFNames=AW12_00022 {ECO:0000313|EMBL:EXI93166.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI93166.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI93166.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:EXI93166.1}.
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DR EMBL; JEMZ01000001; EXI93166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011Q0A8; -.
DR STRING; 1454005.AW12_00022; -.
DR PATRIC; fig|1454005.3.peg.22; -.
DR Proteomes; UP000020878; 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:EXI93166.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878}.
FT DOMAIN 21..154
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 166..403
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 79..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 766 AA; 83963 MW; 36B4C543DF0492A2 CRC64;
MKKPGEQLRT AALFYHRNPK PGKVAIQPTK QLANQYDLSM AYSPGVAAAC EEIAAAPAEV
STLTSRANLV GVITNGTAVL GLGAIGPLAA KPVMEGKAVL FKKFANIDAF DLEIEERDPD
RLVEIVASLE PTFGGINLED IKAPECFHVE QKLRQRMKIP VFHDDQHGTA IVVGAAILNG
LFLQGKELDQ VKLVTSGAGA AALACLDLLV MLGLPVDNVW VTDIKGLVYQ GRVDEMDEIK
ARYAKRTDAR TLGEVIVGAD VFLGLSAGGV LKPEMVAQMA ASPLIMALAN PQPEIRPEDV
KVVRDDAIIA TGRSDYPNQV NNVLCFPFIF RGALDVGATT INDAMKLAAV RAIAELARVE
QSEVALKAYG EKHANFGPEY LIPNPFDPRL IGKIAPAVAE AAMESGVASR PLKDLEAYRE
SLHEFVYHFG LIMKPVFSQA KQAPRRVVFA EGEDDRVLRA IQVIVDEGIA RPILIGHPSE
IERKLEALNL RVTPDDDFDI VYADNNGFFD EHFESYWREY RRLMERKGVS ADFARREVRR
RASLFGAMMV RMGDADGLIC GTFGRHDVHR EYVENVIGLA PGVSDLYAMS LLVLPDRTLF
IADTYINYEP SAEQLADMTL LAADEVRRFG IQPRVALLSH SSFGSENTPT AIKMRRTLKL
LKERAPRLEV EGEMHGDAAL DEHIRQRVFP SDARLKGQAN LLIMPTLDAA NISFNLLKIA
SGDNLTIGPI LLGAAQPVHI LTSTATVRRI VNMTALTVVD KLMNER
//
