ID B1FGX5_9BURK Unreviewed; 756 AA.
AC B1FGX5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+))., Phosphate acetyltransferase {ECO:0000313|EMBL:EDT03200.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EDT03200.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:EDT03200.1};
GN ORFNames=BamIOP4010DRAFT_3285 {ECO:0000313|EMBL:EDT03200.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT03200.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT03200.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT03200.1,
RC ECO:0000313|Proteomes:UP000005463};
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
RT IOP40-10.";
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: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:EDT03200.1}.
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DR EMBL; ABLC01000080; EDT03200.1; -; Genomic_DNA.
DR RefSeq; WP_006752464.1; NZ_ABLC01000080.1.
DR AlphaFoldDB; B1FGX5; -.
DR PATRIC; fig|396596.7.peg.4388; -.
DR Proteomes; UP000005463; 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; IPR001891; Malic_OxRdtase.
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 PRINTS; PR00072; MALOXRDTASE.
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:EDT03200.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2,
KW ECO:0000256|RuleBase:RU003427};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EDT03200.1}; Transferase {ECO:0000313|EMBL:EDT03200.1}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
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 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 756 AA; 81028 MW; F0040D72ED5EA35D CRC64;
MDEQLKQAAL AYHLNPKPGK ISVTPTKPLS NQLDLSLAYS PGVAAACEAI HADPLDAQKY
TSRGNLVGVI TNGTAVLGLG NIGPLAAKPV MEGKGCLFKK FAGIDVFDIE LSESDPDKLV
EAIAMLEPTL GGINLEDIKA PECFYIEQKL RERMKIPVFH DDQHGTAIIA SAAILNGLKV
VGKKLAEVKL VCSGAGAAAI ACLDLLVNLG LTKSNILVAD SKGVIYEGRG NLDPSKQRYA
ATTDARTLAD AIVGADVFLG CSSAGVLKQD MVKTMGDRPL ILALANPEPE IRPEDAKAVR
PDAIVATGRS DYPNQVNNVL CFPFIFRGAL DVGATTITEE MKLACVRAIA ELAQETEQSE
EVAKAYEGHS LEFGPEYLIP KPFDPRLIIK IAPAVAQAAM DSGVATRPIQ DMDAYREQLG
ATVYRTGMVM RPVFATAKQK QARIVFAEGE DERVLRAAQF VLLEKIAKPI IIGRPSVVEM
RLQKIGSKLK AGVDFEIVNP EDDTRYHRYW QAYHEIGARD GVTPEVAKAA LRKFNTLIGA
MLVHLGDADG MICGMIDTYH THLKFIEQVL GRANGAEHYA AMNLLMLPGR NLFMCDTYVN
EVPSAEQLAD MTIQAAAEIE RFGITPKAAL LSNSNFGSAP SSSSRRMAEA RKLISERAPN
LEVDGEMHGD AALSEAVRKA AFPGTTLSGE ANLLIMPNVE AANIAYNLLK MVGGEGVTVG
PFLLGAAKPV HILTPAATVR RIINMTAVAA ANANTK
//