ID A0A1A9NGZ1_9BURK Unreviewed; 779 AA.
AC A0A1A9NGZ1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OAJ65690.1};
GN ORFNames=A6V37_14015 {ECO:0000313|EMBL:OAJ65690.1};
OS Paraburkholderia ginsengiterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ65690.1, ECO:0000313|Proteomes:UP000078116};
RN [1] {ECO:0000313|EMBL:OAJ65690.1, ECO:0000313|Proteomes:UP000078116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY85 {ECO:0000313|EMBL:OAJ65690.1,
RC ECO:0000313|Proteomes:UP000078116};
RA Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL Submitted (APR-2016) 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:OAJ65690.1}.
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DR EMBL; LXKA01000022; OAJ65690.1; -; Genomic_DNA.
DR RefSeq; WP_064268870.1; NZ_LXKA01000022.1.
DR AlphaFoldDB; A0A1A9NGZ1; -.
DR STRING; 1462993.A6V36_05995; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000078116; 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}.
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; 84664 MW; C2E595EE941532B4 CRC64;
MPSNVYSNPH FEARPMSTPV NSKLREAALD YHEFPTPGKI AIAPTKQMIN QRDLALAYSP
GVAFACEEIV ENPLNAARFT ARSNLVGVVT NGTAVLGLGN IGPLASKPVM EGKAVLFKKF
AGIDVFDIEL NESDPHKLVE VIAALEPTFG GINLEDIKAP DCFIVERECR KRMKIPVFHD
DQHGTAIVVA AAVTNGLKVV GKDIKNVKLV ASGAGAAALA CLDLLVDIGL PLENITVTDL
AGVVYKGRVE LMDPDKERFA RETSARTLAE AIGGADIFLG LSAGGVLKQD MVKQMADKPL
ILALANPTPE ILPELALEVR PDAVLCTGRT DYPNQVNNVL VFPFLFRGAL DAGATTVTRE
MEIAAVNAIA ELARQEQSDI VATAYGIQDL SFGPQYLIPK PFDPRLIVKV APAVAKAAMD
SGVAERPIED MEAYEQHLQQ FVYHSGTTMK PIFQVARSVE PEKKRIVFAE GEEERVLRAM
QIVVDEKLAK PILIGRPAVI EQRIARYGLR LVAGQDYSVV NTDHDERYRD FWQEYHKMMS
RKGISAQMAK LEMRRRTTLI GAMLVEKGEA DGMICGTVST THRHLHFIDQ VIGKKAGAKV
YAAMNGLVLP NRQIFLVDTH VNVDPTPEEL AEITIMAAEE VRRFGIEPKI ALLSHSNFGT
SNAPSAQKMR DTLAILRERA PHLQVDGEMH GDIALDANLR REAMPDSTLE GDANLLVLPN
IDAANISYNL LKTAAGNNIA IGPMLLGAAK PVHVLTASAT VRRIVNMTAL LVADVIAAR
//
