MAEB_HALED
ID MAEB_HALED Reviewed; 422 AA.
AC E1V8J1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=NADP-dependent malic enzyme {ECO:0000250|UniProtKB:P40927};
DE Short=NADP-ME {ECO:0000250|UniProtKB:P40927};
DE EC=1.1.1.40 {ECO:0000269|PubMed:28081159};
DE AltName: Full=Malic enzyme {ECO:0000303|PubMed:28081159};
GN Name=maeB {ECO:0000303|PubMed:28081159};
GN OrderedLocusNames=HELO_3763 {ECO:0000312|EMBL:CBV43647.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA Kunte H.J.;
RT "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT study for integrative systems biology.";
RL PLoS ONE 12:E0168818-E0168818(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC Evidence={ECO:0000269|PubMed:28081159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.40; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P40927};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P40927};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250|UniProtKB:P40927};
CC -!- INDUCTION: Up-regulated by salt. {ECO:0000269|PubMed:28081159}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; FN869568; CBV43647.1; -; Genomic_DNA.
DR RefSeq; WP_013333519.1; NC_014532.2.
DR AlphaFoldDB; E1V8J1; -.
DR SMR; E1V8J1; -.
DR STRING; 768066.HELO_3763; -.
DR EnsemblBacteria; CBV43647; CBV43647; HELO_3763.
DR KEGG; hel:HELO_3763; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_6; -.
DR OMA; HKYAAVV; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_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; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..422
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000439541"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT SITE 162
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT SITE 236
FT /note="Confers specificity for NADP"
FT /evidence="ECO:0000250|UniProtKB:P40927"
SQ SEQUENCE 422 AA; 45328 MW; BF399A79EA5929E1 CRC64;
MTDAKRQAAL DYHAKPIPGK LSVELTKPTA TARDLALAYS PGVAEPVREI ARDPENAYLY
TGKGNLVAVI SDGSAILGLG NLGPLASKPV MEGKGVLFKR FAGINSIDVE VDAESPQAFI
DTVARIADSW GGINLEDIKA PECFEIERAL VEQCNIPVFH DDQHGTAIVT AAGMLNALDI
AGKSLESARI VCLGAGAAAI ACMKLLVACG ARSENLVMLD RKGVIHSGRE DLNQYKAMFA
IDTDKRTLAD AIEGADVFVG LSGPGLMTEE HIRRMADNPV VFACTNPDPE IHPDLARETR
PDVIMATGRS DYPNQVNNVL GFPFIFRGAL DVRATRINED MKVAAVHALK DLAREPVPQA
VLEAYDKDAM SFGRDYIIPT PIDVRLLERV SSAVAQAAVD SGVARRPYPA HYPLKTVDDV
YG
