ID A0A1Y5E1Y3_9PROT Unreviewed; 754 AA.
AC A0A1Y5E1Y3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:OUR76230.1};
GN ORFNames=A9Q83_15615 {ECO:0000313|EMBL:OUR76230.1};
OS Alphaproteobacteria bacterium 46_93_T64.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1856292 {ECO:0000313|EMBL:OUR76230.1, ECO:0000313|Proteomes:UP000196525};
RN [1] {ECO:0000313|Proteomes:UP000196525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT within a complex community of hydrocarbon-degraders.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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:OUR76230.1}.
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DR EMBL; MAAN01000035; OUR76230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5E1Y3; -.
DR Proteomes; UP000196525; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 754 AA; 81850 MW; 314BB1DF21F57DFB CRC64;
MSDTRDSSQY DEALRYHAQG KPGKMEIVAT KSVATQQDLS LAYSPGVAAP CLAIVEDPDT
VYDYTTKGNR VAVITNGTAV LGLGNLGALG SKPVMEGKAV LFKRFADLDC FDLELDTEDV
DEFVNSVRLM GPSFGGINLE DIKAPECFII EQRLRELMDI PVFHDDQHGT AIICAAGVIN
ALDLTGRKIE DVKIVVNGAG AAAIACLELI KAMGLPHSNA ILCDTKGVIY KGREEGMNQW
KSAHAVETDH RTLAEAMVGA DIFLGLSVKD AVTKSMVKEM AAKPIIFAMA NPDPEIRPEE
IAEVRGDAIV ATGRSDFPNQ VNNVLGFPYI FRGALDVRAT TINEEMKIAA AEALAELARE
DVPDEVAAAY KGNRPVYGPG YIIPVPFDPR LITHVPMAVA KAAMETGVAR KPIIDEAAYR
NELRARLDPT AGSLQMIMDE VRANPRRVVF AEGEEEKVIR AAIEFKKAGY GVPVLIGRDA
VIKETMASVG IALDEDIEIY NALEMDDREK YHDFLYERLQ RKGYLYRDCV RLVNRDRNIF
GACMVASGDA DAMVTGVTRR FSVSFKEIVK VIDPKENQKV IGVSIAVGRD RTVFIADTAV
TTLPSAQELV NITKEAAEVA RRMGHEPRVA LLSYSNFGNP AHATTESMRE AVKLLDQQEL
DFEYDGEMSA DVALNPEIMA LYPFCRLSGP ANVLVMPGLH SAHITSKLIS VMGETKVIGP
LMVGLSKPVQ IVPIGATVSD LVNMAALAAH EAGQ
//
