ID B1T9M6_9BURK Unreviewed; 780 AA.
AC B1T9M6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+))., Phosphate acetyltransferase {ECO:0000313|EMBL:EDT39743.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EDT39743.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:EDT39743.1};
GN ORFNames=BamMEX5DRAFT_4492 {ECO:0000313|EMBL:EDT39743.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT39743.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT39743.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT39743.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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:EDT39743.1}.
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DR EMBL; ABLK01000169; EDT39743.1; -; Genomic_DNA.
DR AlphaFoldDB; B1T9M6; -.
DR PATRIC; fig|396597.7.peg.3308; -.
DR Proteomes; UP000004814; Unassembled WGS sequence.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
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 Acyltransferase {ECO:0000313|EMBL:EDT39743.1};
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,
KW ECO:0000313|EMBL:EDT39743.1}; Transferase {ECO:0000313|EMBL:EDT39743.1}.
FT DOMAIN 38..171
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 183..420
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 96..103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 307
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 780 AA; 84725 MW; 0FD3FD6370DB9812 CRC64;
MPSNSYSNPH VKRHMSTQAS SKAKLREAAL DYHEFPTPGK IAIAPTKQMI NQRDLALAYS
PGVAYACEEI VENPLNAARF TARSNLVGVV TNGTAVLGLG NIGPLASKPV MEGKAVLFKK
FAGIDVFDIE LNESDPHKLV DVIAALEPTF GGINLEDIKA PDCFIVEREA RKRMKIPVFH
DDQHGTAIVV AAAVTNGLKV VGKDIKKVKL VASGAGAAAL ACLDLLVDIG LPIENILVTD
LAGVVYKGRA ELMDPDKERF ARETEARTLA EVIDGADIFL GLSAAGVLKQ EMVKGMAERP
LILALANPTP EILPELALEV RPDAVLATGR TDYPNQVNNV LCFPFIFRGA LDVGATTITR
EMEIAAVNAI AELAQQEQSD IVATAYGIQD LSFGPEYLIP KPFDPRLIVK IAPAVAQAAM
DGGVATRPIE DMEAYRVHLQ QFVYHSGTTM KPIFQIARAA PAEKKRVVFA EGEEERVLRA
VQIIVDEKLA KPILIGRPSV IEHRIQRYGL RLTPGTDFTV VNTEHDERYR DFWQTYYKMM
SRKGISEQLA RVEMRRRTTL IGSMLVKKGE ADGMICGTIS TTHRHLHFID QVIGKRPGCS
VYAAMNGLVL PGRQIFLVDT HVNVDPTPEE LAEITIMAAE EVRRFGIEPK VALVSHSNFG
TSNAPSAKKM RDTLAILQER APELKVDGEM HGDVALDAAL RKEILPESTL EGDANLLILP
NIDAANIAYN LLKTAAGNNI AIGPILLGAA QPVHVLTESA TVRRIVNMAA LLVADVNAAR
//
