ID A0A432CEX8_9FLAO Unreviewed; 758 AA.
AC A0A432CEX8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RTZ00340.1};
GN ORFNames=EKM02_08545 {ECO:0000313|EMBL:RTZ00340.1};
OS Flavobacterium sp. RSP49.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTZ00340.1, ECO:0000313|Proteomes:UP000272024};
RN [1] {ECO:0000313|EMBL:RTZ00340.1, ECO:0000313|Proteomes:UP000272024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSP49 {ECO:0000313|EMBL:RTZ00340.1,
RC ECO:0000313|Proteomes:UP000272024};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (DEC-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:RTZ00340.1}.
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DR EMBL; RYDN01000013; RTZ00340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432CEX8; -.
DR Proteomes; UP000272024; 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}.
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 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 758 AA; 82888 MW; AF3F8DDB5F866F36 CRC64;
MEKNSKRREA LLYHAKPTPG KIQVVPTKKY ATQRDLSLAY SPGVAEPCLE IAKDVNNVYK
YTAKGNLVAV ITNGTAVLGL GDIGPEASKP VMEGKGLLFK IFANIDVFDI EIGTKDIEEF
IQTVKNIAPT FGGINLEDIK APESFEIERR LVEELNIPVM HDDQHGTAII SSAALLNALE
LAGKNVEDVK LVVSGAGSAA LACANLYILL GVKLENILMY NSKGLLTKDN PKLSDLQLKY
AKDILPISLE EALVGADVFL GLSSGDIMTP KMLQGMAINP IVFAMANPDP EIDYNLAIAT
RKDVIMATGR SDYPNQVNNV LGFPYIFRGA LDVRATKINE AMKMAAVRAL AALAKESVPE
QVNIAYGAKK LTFGRDYIIP SPFDPRLIIV VAPAVAKAAM DSGVALNPIT DWVKYEEELL
ERLGNDNKMV RLITNRAKMD PKKIVFAEAD HLDVLKAAQI VLEEGIGFPV LLGNKEIILE
LKAEIGFDAD VEIIDPKITE EEDRRNKFAT TYWASRQRRG ISLLDAQKLM RERNYFAAMM
VNEGEADALV TGYSRSYPTV VKPILQLIEK APGASLVATT NMMMTARGPM FLSDTAININ
PSADDLAKIA VMTAKTARMF GVEPVIAMIS YSNFGSSSNE SATKVRQAVA YLHENHPEMI
IDGELQADFA LNPEMLKEKF PFSKLAGKKV NTLIFPNLES ANITYKLLKE LNKVDSIGPI
MLGMGKPVHI FQLGASVEEM VNMAAIAVID AQEKQKKK
//
