ID A0A1Y5T0F1_9RHOB Unreviewed; 750 AA.
AC A0A1Y5T0F1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:SLN50855.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:SLN50855.1};
GN Name=tme {ECO:0000313|EMBL:SLN50855.1};
GN ORFNames=PAM7066_02308 {ECO:0000313|EMBL:SLN50855.1};
OS Palleronia marisminoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=315423 {ECO:0000313|EMBL:SLN50855.1, ECO:0000313|Proteomes:UP000193870};
RN [1] {ECO:0000313|EMBL:SLN50855.1, ECO:0000313|Proteomes:UP000193870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7066 {ECO:0000313|EMBL:SLN50855.1,
RC ECO:0000313|Proteomes:UP000193870};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; FWFV01000006; SLN50855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T0F1; -.
DR STRING; 315423.SAMN04488020_10675; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000193870; 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; IPR015884; Malic_enzyme_CS.
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.
DR PROSITE; PS00331; MALIC_ENZYMES; 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 ECO:0000313|EMBL:SLN50855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193870}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 77..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 288
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 750 AA; 81085 MW; 015B490842EEFCEE CRC64;
MAKKFTDEEA LQFHMQPRPG KFDIAASVPM STQRDLSLAY SPGVAVPCER IAAEPGQAYD
YTNKGNLVAV ISNGTAVLGL GNLGALASKP VMEGKAVLFK RFADVNSIDI ELATEDPDAF
CAAVKLMEPT FGGINLEDIK APECFIIESR LKEEMDIPVF HDDQHGTAVI CAAGLINALH
ISGKRIEDVR IVLNGAGAAG IACLELLKAM GATADNCIMC DTKGVIYQGR TEGMNQWKSA
HAARTDLRTL EQAMDGADVF LGVSVKGAVT QKMVESMAPN AVIFAMANPD PEITPEDVHA
VREDVIVATG RSDYPNQVNN VLGFPYLFRG ALDIHARAIN DEMKIACAEA LAALAREDVP
DEVALAYGRS LKFGRDYIIP TPFDPRLIWR IPPAVARAGM DTGVGRRPIV DMEGYQQALK
ARMDPTASIL QGIYARARRA QKRMIFAEGD DIRVLRAALA YRREGLGEAI VVGRDADIRE
KLHTEGLGSA FDGLNIVNAA KTEHLETYKD FLYERLQRKG YDRSDIHRMA ARDRHVFSAL
MLAHGHGDAL VTGATRKSAH VLDQINMVFD ARAEDGAVGI TALSLRGRIV LIADTLVHEW
PDEDDLANIA SRGADVARAL GLEPRVAFVS FSTFGYPVSE RARKMHLAPQ VLDARGADFE
YEGEMTVDVA LNTEAMKHYP FCRLTGPANV LVVPARHSAS ISVKLMQEMG GATVLGPILT
GIAKPVQIAS TGMGVADILN MAAIAARDMA
//
