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
//