ID A0A1N7ADA6_9BACT Unreviewed; 757 AA.
AC A0A1N7ADA6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SIR36974.1};
GN ORFNames=SAMN05421545_3390 {ECO:0000313|EMBL:SIR36974.1};
OS Pontibacter lucknowensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1077936 {ECO:0000313|EMBL:SIR36974.1, ECO:0000313|Proteomes:UP000185924};
RN [1] {ECO:0000313|Proteomes:UP000185924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM9 {ECO:0000313|Proteomes:UP000185924};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; FTNM01000005; SIR36974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7ADA6; -.
DR STRING; 1077936.SAMN05421545_3390; -.
DR Proteomes; UP000185924; 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; 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; IPR001891; Malic_OxRdtase.
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 PRINTS; PR00072; MALOXRDTASE.
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 Reference proteome {ECO:0000313|Proteomes:UP000185924}.
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 757 AA; 83295 MW; 009F710E4B640CEB CRC64;
MIKVNKEDAL NYHMQGQPGK IEVVPTKMLS TQHDLALAYS PGVAEPCKEI AADKENVYKY
TAKGNLVGVI SNGTAVLGLG NIGPDASKPV MEGKGVLFKK FAGIDVFDIE IDCTDPEEFI
RIVKSLEPTF GGINLEDIKA PESFKIENAL KEQMNIPLMH DDQHGTAIIS AAALLNALEL
AGKRIEEVQI VMNGAGAAAI ACAKLYVALG AKLDNIVMFD KDGIIRPERN DLDIYRAQFV
TLRKINTLAE AMKGADVFIG LSAGNVLDPE LVKLMANDPI IFALANPDPE IPYAVAMETR
EDLIMATGRS DHPNQVNNVL GFPYIFRGAL DVRATEINEA MKLAAVRALA DLAKEPVPEM
VHKAYGDNTI SFGRTYLIPK PLDPRLITTV SPAVAKAAIE SGVAKHPITN WEAYETELQE
RIGIDQKLMT RITNQAKKNP KTVVFAEADH YKILKAAQIV KEQRIANPIL LGNKARIAAI
IEETNLDLHD CVIIDPYEEE QKREEFAQLL YAKRQRKGLT LFDSRRQMRD RNYFGAMMLE
TGEADALISG LTRDYSKTIL PSLQIIGVEE GINKVAGMYI ILSKKEPYFF ADTTVNVNPT
ADELVDIIGL TARAVRFFDT EPRMAVLSYS NFGSVQGDIP NKGAEAVRKA KQRYPDLMID
GEMQANTAMN RHLLKEHYPF SELADKGANT LIFPTLTSGN IAYKLLQEIG GAEAIGPVLM
GMRKPVHILQ LGSSIREIVN MVAIAVVDAQ NYNNKHI
//
