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Database: UniProt
Entry: A0A1V3ICQ2_9PAST
LinkDB: A0A1V3ICQ2_9PAST
Original site: A0A1V3ICQ2_9PAST 
ID   A0A1V3ICQ2_9PAST        Unreviewed;       756 AA.
AC   A0A1V3ICQ2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:OOF37715.1};
GN   ORFNames=BKK48_00315 {ECO:0000313|EMBL:OOF37715.1};
OS   Rodentibacter heidelbergensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1908258 {ECO:0000313|EMBL:OOF37715.1, ECO:0000313|Proteomes:UP000189437};
RN   [1] {ECO:0000313|EMBL:OOF37715.1, ECO:0000313|Proteomes:UP000189437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac69 {ECO:0000313|EMBL:OOF37715.1,
RC   ECO:0000313|Proteomes:UP000189437};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-2016) 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:OOF37715.1}.
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DR   EMBL; MLHH01000002; OOF37715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3ICQ2; -.
DR   STRING; 1908258.BKK48_00315; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000189437; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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: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          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..401
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         76..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         162
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   756 AA;  81812 MW;  EF0E7262ADA08157 CRC64;
     MSEQLRQAAL DFHEFPIPGK IEVTPTKSLA TQRDLALAYS PGVAEPCLEI EKDPLASYKY
     TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGINVFDIE VNEHDPDKLV
     DIIASLEPTF GGINLEDIKA PECFYIEQKL RERMNIPVFH DDQHGTAIIS AAAIINSLRI
     IGKKIEEVRL VASGAGAASI ACLNLLLSLG MKRENITICD SKGVVYKNRG DRMDKTKEDY
     AIEDNGWRSL ADAIPNADIF LGCSAAGALT QDMVKTMAAH PIILALANPN PEITPPEAKA
     VRPDAIVCTG RSDYPNQVNN VLCFPFIFRG ALDVGATTIN EEMKRAAVYA IADLALEEQN
     EVVTSAYGGE GATFGADYVI PRPFDPRLIV RIAPAVAKAA MDSGVATRPI SDWNEYSEKL
     TQFVYKTSLF MRPIFSQAKS AKQRIILAEG EETKALHAVQ EVVSMELASP ILIGRKAVIE
     EKIKKLGLRL EVGVNVEVVD NENNPRYEEC WKYYYQLTKR KGITPAIAKR VVRSNTTVLA
     SVLVNLGYAD GLVCGLFGSY GKHLDSIRDI IGLKEGVKTV AALNSLVLPS GNVFLTDTHV
     NDDPSAEELA EITLMAADEV HRFGIEPAVA LLSHSNFGSS NTLGAPKVRE ALKRVQEHHP
     QLMIDGEMRG DIALCAAQRT EVMPDSPLKG SANLLVFPNL SAARISYSLL RGTTTAVTVG
     PILMGMNKSA HILNPSASVR RIINMVAYAA VKAQQD
//
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