ID A0A2P8D616_9BACT Unreviewed; 760 AA.
AC A0A2P8D616;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:PSK92629.1};
GN ORFNames=B0I18_103206 {ECO:0000313|EMBL:PSK92629.1};
OS Taibaiella chishuiensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Taibaiella.
OX NCBI_TaxID=1434707 {ECO:0000313|EMBL:PSK92629.1, ECO:0000313|Proteomes:UP000240572};
RN [1] {ECO:0000313|EMBL:PSK92629.1, ECO:0000313|Proteomes:UP000240572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12700 {ECO:0000313|EMBL:PSK92629.1,
RC ECO:0000313|Proteomes:UP000240572};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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: 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:PSK92629.1}.
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DR EMBL; PYGD01000003; PSK92629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8D616; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000240572; 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; 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.
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:UP000240572}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
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; 83652 MW; 6EC891C1CA727941 CRC64;
MNNRKIDPQD ALDYHSQGRP GKIKVVPTKN TKTQRDLSLA YSPGVAEPCL AIRDNPEDVY
KYTAKGNLVA VISNGTAVLG LGDIGPEAGK PVMEGKGVLF KIFADIDVFD IELNANDVER
FIDVVKALEP TFGGINLEDI KAPECFEIER RLKQELKIPV MHDDQHGTAI ISAAALLNAL
ELVDKKIEEV KFVVNGAGAA AIACAKLYIS LGARKENILM LDSKGVINAT RTGLDEMKQE
FVVDTPLETL EDAMRGSDVF IGLSKADVLS QDMVRSMADR PIVFAMANPN PEIGYDEALA
ARPDVIMATG RSDYPNQVNN VLGFPFIFRG ALDVRATQIN EAMKLAAVRA LAELTRQPVP
DMVNMAYGEK NMTFGAQYII PKPLDPRLLT AVAPAVAKAA MESGVARQPI TDWEKYHQEL
SARLGLDNYT VRVLNNTARK DPRRVVFAEA DNAKVLKAAQ IVKDEGIAIP ILLGNESKIR
QILDDNSIDL KDVTIIDPRS EAMLETRIRY GEQFFEKRYR RGFNIYEAKK IMRERNYFGC
MMVENGEADA LISGLTRSYP DTIRPALEVI GLEEGVKKVA GMYIILRPQG PLFLADTTVN
LNPTAEELAD ITLLTAKEVR QFNIEPRIAM LSYSNFGSSR TPEAMMVRDA LQIVKDKDPG
LIVDGELQAS MAFNRDILKE SYPFSPLIDG EVNTLIFPNL AAGNIAYNLL MEVGGFEVIG
PVLMGLKKPV HILQLGSSVR QICSMVAMAV MDAQVKCSKK
//
