ID A0A3E2NJN6_9SPHI Unreviewed; 760 AA.
AC A0A3E2NJN6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RFZ81216.1};
GN ORFNames=DYU05_19725 {ECO:0000313|EMBL:RFZ81216.1};
OS Mucilaginibacter terrenus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2482727 {ECO:0000313|EMBL:RFZ81216.1, ECO:0000313|Proteomes:UP000260823};
RN [1] {ECO:0000313|EMBL:RFZ81216.1, ECO:0000313|Proteomes:UP000260823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZH6 {ECO:0000313|EMBL:RFZ81216.1,
RC ECO:0000313|Proteomes:UP000260823};
RA Huang Y., Zhou Z.;
RT "Mucilaginibacter terrae sp. nov., isolated from manganese diggings.";
RL Submitted (AUG-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:RFZ81216.1}.
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DR EMBL; QWDE01000006; RFZ81216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2NJN6; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000260823; 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 Reference proteome {ECO:0000313|Proteomes:UP000260823}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..401
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 760 AA; 83211 MW; A450869BFEED8B40 CRC64;
MNKANRKQDA LNYHAKGRPG KIEVVPTKPT NTQRDLTLAY SPGVAEPCRA IAENVDDVYK
YTAKGNLVAV ISNGTAVLGL GNIGPEASKP VMEGKGLLFK IYADIDVFDL EVNAKSVDDF
VNIVKALEPT FGGVNLEDIS APTCFEIERR LKAEMNIPVM HDDQHGTAII SGAALMNACE
IQGKKLEEIK MVVNGAGAAA VSCTKMYLSL GVKKENIVMF DINGLLSTNR TDLDDIRKEF
ATTRTDIENL ADAMKNADVF VGLSAGNVVT QEMLVTMAEN PVVFAMANPE PEISYDLATA
ARTDIIMATG RSDYPNQVNN VLGFPYIFRG ALDVRATAIN EEMKIAAVKA IAEMAKRPVP
EAVNLAYNTT NLKFGRDYII PKPMDQRLIT EVSSAVAKAA INSGVARKVI TDWDAYHEEL
LSRLGTNNKL MRDITNKAKQ SPKRVVFAEA DTYKILRAAQ IVKDEGIATP ILLGNIQKIK
QIMYDNELDL GEVEMIDTRD ECDRKKDFAE FLYKKRQRRG ITLSEAKKLV TDRNYYGACM
VQFGQADALI SGLTKNYADT IKPALQVIGT DEGVNRVAGM YLMITEKGPV FFGDTTVNIN
PTVEELVDIT VLVEKAVSYF ISKPRVALLS YSNFGSNKGD IPDKTAEAVR ILHQRYPNMV
VDGEMQANFA LNAELLKDNF AFSTLNGKPA NTLIFPTLAS GNIAYKLLQE IGGAEAVGPI
LLGLKKPVHV LQLGSSVREI VNMVTIAVVD AQEKDRTTNR
//
