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Database: UniProt
Entry: A0A0U2YDW4_9BURK
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ID   A0A0U2YDW4_9BURK        Unreviewed;       762 AA.
AC   A0A0U2YDW4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ALS62981.1};
GN   ORFNames=AT302_02530 {ECO:0000313|EMBL:ALS62981.1};
OS   Pandoraea norimbergensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93219 {ECO:0000313|EMBL:ALS62981.1, ECO:0000313|Proteomes:UP000060277};
RN   [1] {ECO:0000313|Proteomes:UP000060277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11628 {ECO:0000313|Proteomes:UP000060277};
RA   Ee R., Lim Y.-L., Yong D., Yin W.-F., Chan K.-G.;
RT   "Complete genome sequence of Pandoraea norimbergensis DSM 11628.";
RL   Submitted (DEC-2015) 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; CP013480; ALS62981.1; -; Genomic_DNA.
DR   RefSeq; WP_058379836.1; NZ_CP013480.3.
DR   AlphaFoldDB; A0A0U2YDW4; -.
DR   STRING; 93219.AT302_02530; -.
DR   KEGG; pnr:AT302_02530; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000060277; Chromosome.
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          19..152
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          164..401
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         288
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   762 AA;  82241 MW;  39E290C42840D71B CRC64;
     MSNNNDHQAA LEYHQFPTPG KISVTASKPL VTQRDLALAY TPGVAIPCQE IAADPAKAFN
     YTARGNLVGV ITNGSAVLGL GNIGALASKP VMEGKAVLFK KFAGIDVFDI EITESDPDKL
     VEIIASLEAT FGGINLEDIK APECFTVERK LRERMKIPVF HDDQHGTAIT VSAAFINGLK
     VVGKDIKEVK VVTSGAGAAA LACLDLMVDL GLPIENVWAT DIDGVVYEGR AVGMDPDKAR
     FAQKTDKRTL AEVIDGADVF LGLSAGGVLK PEMLKTMGPR PLILALANPT PEIFPEDARA
     ARDDVVLATG RSDFPNQVNN VLCFPYIFRG ALDVGATTIT RNMEIAAVNA IAALAQEEPN
     DSVATAYGAY DLSFGPEYLI PKPFDSRLIV RIAPAVARAA MEDGVATRPI ADFDAYADQL
     QQFVYHSGAF MKPIFSAAKQ LVRDGGKARI VFAEGEEERV LRAVQVIVDE KLARPILVGR
     PEVLLARIEK FGLRLRLGED VEVTNPYYDE RFHQYWTSYW ELRCRDGITK EMARVEMRRR
     LTLIGAMMVR LGDADGMICG TVGAYHDHLR FVDEVIGKQA GANTYAAMNI LLLDKRTVAL
     VDTHVNDDPT AEQIAEFTIA AAKQMSWLNL NPKVALLSRS NFGSGSAASG TKMRRVLDLV
     SAQAPDLEID GEMHGDCALD EGLRSRILPH SRLKGAANLL VCPNVDSGNI AYNLLKTGAG
     SNVAVGPFLL GVGAPVNVLT SSSTVRRIIN MTALTVIQAN RD
//
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