ID A0A1I3FPD1_9SPHI Unreviewed; 762 AA.
AC A0A1I3FPD1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SFI13016.1};
GN ORFNames=SAMN05444682_102428 {ECO:0000313|EMBL:SFI13016.1};
OS Parapedobacter indicus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=1477437 {ECO:0000313|EMBL:SFI13016.1, ECO:0000313|Proteomes:UP000198670};
RN [1] {ECO:0000313|EMBL:SFI13016.1, ECO:0000313|Proteomes:UP000198670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK1 {ECO:0000313|EMBL:SFI13016.1,
RC ECO:0000313|Proteomes:UP000198670};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOQO01000002; SFI13016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3FPD1; -.
DR STRING; 1477437.SAMN05444682_102428; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000198670; 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:UP000198670}.
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 762 AA; 83713 MW; F064910DD059DD26 CRC64;
MSKTNRKQDA LDYHAKGRPG KIAVIPTKPT HSQRDLSLAY SPGVAEPCLR IAENTEDVYK
YTAKGNLVAV ISNGTAVLGL GDIGPEAGKP VMEGKGLLFK IFADIDVFDI ELNTKNVDEF
VRMVKCLEPT FGGVNLEDIK APECFEIERR LKEELNIPVM HDDQHGTAII SGAALVNACA
LQKKKIERVK IVVNGAGAAA ISCTRMYIAL GARKENIVML DSKGCIREDR GNLDPTKAEF
ATSQKIETLE EALKGADVFI GLSIADVVTP EMLKSMAKNA IVFAMANPNP EISYPLAIET
RKDVIMATGR SDYPNQVNNV LGFPYIFRGA LDVRATVINE EMKIAAVKAL AELAKKPVPE
AVNQAYDTHN LKFGPEYIIP KPTDPRLITE VSLAVAKAAM DSGVARKAIT DWDKYAEELR
QRLGQDDRIM RNLTEAAKRD PKRVVFAEAD NYKTLRAAQI VKEEGIAIPI LLGNKRKIQQ
LIDENLLELG EVEIIDPLEE KGNPRFLSYV EFLYTKRQRR GVSYLDAQKL MLDRNYFGAS
MVQVGEADTL ISGLTKNYAT TIRPALHVIG SQPGSRIAGM YMMLTSKGPV FFGDTTVNAN
PTAEELVDIT LLLHEAVKKM NVTPRIALLS YSNFGSNDGE VPNKTREAAR LLHERHPEIL
VDGEMQANFA MNSDLLASNF PFSSLKGTPA NTLVFPNLES GNIAYKLLQE IGNAEAVGPI
LLGMDKPVHV LQLDSSVREI VNMVTIAVVD VQSRAPMARK KK
//
