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Database: UniProt
Entry: A0A1G6M130_9BACT
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ID   A0A1G6M130_9BACT        Unreviewed;       762 AA.
AC   A0A1G6M130;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SDC48695.1};
GN   ORFNames=SAMN05216323_103337 {ECO:0000313|EMBL:SDC48695.1};
OS   Williamwhitmania taraxaci.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Williamwhitmaniaceae;
OC   Williamwhitmania.
OX   NCBI_TaxID=1640674 {ECO:0000313|EMBL:SDC48695.1, ECO:0000313|Proteomes:UP000199452};
RN   [1] {ECO:0000313|EMBL:SDC48695.1, ECO:0000313|Proteomes:UP000199452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A7P-90m {ECO:0000313|EMBL:SDC48695.1,
RC   ECO:0000313|Proteomes:UP000199452};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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; FMYP01000033; SDC48695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6M130; -.
DR   STRING; 1640674.SAMN05216323_103337; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000199452; 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:UP000199452}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..399
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         76..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         286
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   762 AA;  83041 MW;  032645CF06479249 CRC64;
     MEEGLKREAL DYHAQGRPGK IEVVPTKPNS SQKDLSLAYS PGVAAPCLEI EKNPEDAYKY
     TAKGNLVAVI SNGTAVLGLG DIGALAGKPV MEGKGLLFKT FADIDVFDIE VDTHDIDKFV
     ETVRLIAPTF GGINLEDIKA PECFEIEERL KKLLDIPVMH DDQHGTAIIS SAALLNALTI
     NGKKIEDLIV VVNGAGAAAV ACAKLYFALG IRAENLVMCD SKGAISTRRK DINSIKAQFA
     TQRTVDTLEE AMVGADMFLG LSAANVLTTE MVQSMAKEPI VFALANPDPE IAYDLAMKAR
     PDIIFATGRS DYPNQVNNVL GFPYIFRGAL DVRAKTINEE MKVAAVRALA SLAKEVVPDI
     VANAYNKKTL AFGRDYLIPT PLDPRLISTI SVAVAQAAVK SGVARKTIED WDAYKTELEQ
     RLGYDNAIIR TVRDRTRNSG KRIVFAEGGR LKVLQAAQQI LQEGIATPIL LGSAEKIRKI
     SLDNNIDLNG ATIIEFYGDA EACRREVFAK LFFEKRKRKG ITYQEAIDSM YDRNQFGIMM
     VEVGDADAFI SGYSSKYSTT IKPALQIVGT DNPGNHIAGM YMVMTKQGPI FLADTTVNDQ
     PNAETLVATT LLVDRAVRRF NIEPVIAMVS YSNFGSVPTG QPEISRRAVE ILHANHPEII
     VDGEVQANFA LNKKIRMEKF PFSKWGEKRV NTLVFPDLAS GNISYKLLQE LGGFEVVGPI
     LVGIAKPVHV VPIESSVREI VNMATIAVFD SICTLEGNCG CE
//
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