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Database: UniProt
Entry: A0A2M6V3C2_9BURK
LinkDB: A0A2M6V3C2_9BURK
Original site: A0A2M6V3C2_9BURK 
ID   A0A2M6V3C2_9BURK        Unreviewed;       769 AA.
AC   A0A2M6V3C2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:PIT72942.1};
GN   ORFNames=B9Z42_11555 {ECO:0000313|EMBL:PIT72942.1};
OS   Limnohabitans sp. B9-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1100707 {ECO:0000313|EMBL:PIT72942.1, ECO:0000313|Proteomes:UP000228506};
RN   [1] {ECO:0000313|EMBL:PIT72942.1, ECO:0000313|Proteomes:UP000228506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-3 {ECO:0000313|EMBL:PIT72942.1,
RC   ECO:0000313|Proteomes:UP000228506};
RA   Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA   Simek K., Ghai R.;
RT   "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL   Submitted (APR-2017) 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}.
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:PIT72942.1}.
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DR   EMBL; NESI01000007; PIT72942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M6V3C2; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000228506; 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; IPR032683; Malate_DH.
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; PF12434; Malate_DH; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000228506}.
FT   DOMAIN          29..162
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          174..411
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         87..94
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         147
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         173
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         298
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   769 AA;  83180 MW;  F946737818D23FEF CRC64;
     MSPTPSHNSA EARAELRRAA LEYHEFPTPG KLAIHATKQL VNQHDLALAY SPGVAAPCEE
     IVKDPNNAFK YTSRGNLVAV ITNGTAVLGL GDIGPLASKP VMEGKAVLFK KFAGIDVFDL
     EIDEKNLDKL VDIIASLEPT FGGINLEDIK APDCFYVERK LRERMKIPVF HDDQHGTAIT
     VGAAIINGLK VAGKDIKTVK LVTSGAGAAA LACLGLLLKM GMPRSNIYVT DLAGVVYEGR
     TELMDEDKIQ FAQKTDARTL SDIIEGADVF LGLSAGGVLK PDMVKKMAAK PIIMALANPN
     PEITPEEVKA VRDDAIIATG RSDYHNQVNN VLCFPYIFRG ALDAGASTIT DEMEIAAVYA
     IAELAQAEQS EVVAAAYAGE TLAFGPEYLI PKPFDPRLMM KIAPAVAKAA AASGVATRPI
     QDMDAYIEKL QGFVYASGSI MKPIYAAAKR ASKKRVCYAE GEEERVLRAV QIVVDEGLAK
     PTLIGRPAVI AQRIESFGLR LKEGVDYQVV NVEQDHRYRD FWQTYYKMTC RKGVTEQLAK
     IDMRRRLSLI GTMMLHKGEV DGLICGTWST PLTHLKYVHE VIGNRQGVST YAAMNGLLLP
     DRQVFLVDTH INYDPTAEQL AEITVMAAEE MRRFGIQPKA ALLSHSNFGS SDQPSAIKMR
     ETLALVQKKA PWLEIDGEMH GDVALDGHAR EAQMADTTLI GDANLLVLPN LDAANIAYNL
     LKTAAGGNIA IGPVLLGAAK PVHILTASTT VRRIVNMTAL TVADASAVR
//
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