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Database: UniProt
Entry: A0A3M2HYB4_9GAMM
LinkDB: A0A3M2HYB4_9GAMM
Original site: A0A3M2HYB4_9GAMM 
ID   A0A3M2HYB4_9GAMM        Unreviewed;       761 AA.
AC   A0A3M2HYB4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RMH93235.1};
GN   ORFNames=EBB59_06635 {ECO:0000313|EMBL:RMH93235.1};
OS   Lysobacter pythonis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=2483112 {ECO:0000313|EMBL:RMH93235.1, ECO:0000313|Proteomes:UP000275012};
RN   [1] {ECO:0000313|EMBL:RMH93235.1, ECO:0000313|Proteomes:UP000275012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4284/11 {ECO:0000313|EMBL:RMH93235.1,
RC   ECO:0000313|Proteomes:UP000275012};
RA   Hans-Juergen B., Huptas C., Sandra B., Igor L., Joachim S., Siegfried S.,
RA   Mareike W., Peter K.;
RT   "Proposal of Lysobacter pythonis sp. nov. isolated from royal pythons
RT   (Python regius).";
RL   Submitted (OCT-2018) 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:RMH93235.1}.
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DR   EMBL; RFLY01000007; RMH93235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2HYB4; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000275012; 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; 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.
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:UP000275012}.
FT   DOMAIN          19..152
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          164..399
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        95
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         77..84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         163
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         287
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   761 AA;  82561 MW;  271CD44C3ABB43B6 CRC64;
     MPNEDFKQAA LDYHRQFPPG KIKISATKPM VTQRDLSLAY SPGVAYACEA IVEDANAASE
     MTARGNLVAV ITNGTAVLGL GDIGPLAGKP VMEGKGVLFK KFAGIDVFDI EIDERDPDKL
     IEIIASLEPT FGGINLEDIK APECFIVERK LRERMNIPVF HDDQHGTAII VGSAVLNALE
     VTGKKIEEVR IATTGAGAAG IACLDMLVAL GAKREHIVAF DREGVIYAGR PNLDPDKARY
     ASDTAARTLD EVVAGADIFL GLSAGGILKP EMVAKMADKP IILALANPHP EILPEDAKAV
     RPDAIIATGR SDYPNQVNNA LCFPYIFRGA LDAGATEINE AMKLACVRAI AELARMEASD
     LGGAYGGEIP KFGPEYLIPR PFDPRLITVI APAVAKAAMA SGVSARPIAD MPAYEEKLGQ
     FVHKTGLMMK PVYERARADK KRVVYAEGEE YTVLRGVQTV IDERLAFPVL IGRPEVISRR
     IEKLGLRMRA GRDFELVNLN DDPRFDDYWR AYHRRNARNG ITEDAAKNLI RSRPTLVAAL
     MVERGEADAL ICGLVGRFHK KLGYLRSVFD LEPGVGGTAT MTGVINDHGA WFFVDTHVQA
     DPSAEQIAES ALQASWRLKL FGIEPRVALL SHSNYGSHLD ASAAKMRRAR ELIVERVPKL
     EIDGEMMADT AWDEALRRRI FPDTTLKGRA NLLVMPNLDA ANIGYNLIRV ATGGVAIGPV
     LMGLDKPAHV LTPAATPRRV VNMTAIAAVD AQIRAGLPER E
//
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