ID E1T9F3_BURSG Unreviewed; 779 AA.
AC E1T9F3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Malic protein NAD-binding protein {ECO:0000313|EMBL:ADN58926.1};
GN OrderedLocusNames=BC1003_2974 {ECO:0000313|EMBL:ADN58926.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN58926.1};
RN [1] {ECO:0000313|EMBL:ADN58926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN58926.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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}.
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DR EMBL; CP002217; ADN58926.1; -; Genomic_DNA.
DR AlphaFoldDB; E1T9F3; -.
DR STRING; 640512.BC1003_2974; -.
DR KEGG; bgf:BC1003_2974; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_4; -.
DR OrthoDB; 9805787at2; -.
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}.
FT DOMAIN 37..170
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 182..419
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 95..102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 779 AA; 85009 MW; 3DF155BC62C04C1B CRC64;
MPSNVYSNPH FEARLMSTPV NSKLREAALD YHEFPTPGKL AITPTKQMIN QRDLALAYSP
GVAFACEEIV ENPMNAARFT ARSNLVGVVT NGTAVLGLGN IGPLASKPVM EGKAVLFKKF
AGIDVFDIEL NESDPHKLVD VIAALEPTFG GINLEDIKAP DCFIVERECR KRMKIPVFHD
DQHGTAIVVA AAITNGLKVV GKDIKEVKLV ASGAGAAALA CLDLLVDIGL PLENILVTDL
AGVVYKGRVE LMDPDKERFA RETDARTLAE AIGGADVFLG LSAGGVLKQD MVKQMADKPL
ILALANPTPE ILPELALEVR PDAVLCTGRT DYPNQVNNVL VFPFLFRGAL DAGATTVTRE
MEIAAVNAIA ELARQEQSDI VATAYGIQDL SFGPEYLIPK PFDPRLIVKV APAVAKAAMD
SGVAERPIED MEAYEQHLQQ FVYHSGTTMK PIFQLARSVE PEKKRIVFAE GEEERVLRAM
QIIVDEKLAK PILIGRPAVI EQRIARYGLR LVAGQDYTVV NTDHDERYRD FWQEYYKMMS
RKGITQQMAK LEMRRRTTLI GAMLVKKGEA DGMICGMVST THRHLHFIDQ VIGKREGCAV
YAAMNALVLP NRQIFLVDTH VNVDPTPEQL AEITLMAAEE VRRFGIEPKV ALVSHSNFGS
SHAPTAQKMR DTLAILRERA PELQVDGEMH GDVALDANLR REILPDSTLE GDANLLVLPN
IDAANISYNL LKTAAGNNIA IGPMLLGAAQ PVHVLTASAT VRRIVNMTAL LVADVIAAR
//
