ID B2JIJ5_PARP8 Unreviewed; 761 AA.
AC B2JIJ5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)), Phosphate acetyltransferase {ECO:0000313|EMBL:ACC72041.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ACC72041.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:ACC72041.1};
GN OrderedLocusNames=Bphy_2869 {ECO:0000313|EMBL:ACC72041.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72041.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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}.
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DR EMBL; CP001043; ACC72041.1; -; Genomic_DNA.
DR RefSeq; WP_012402220.1; NZ_CADFGH010000011.1.
DR AlphaFoldDB; B2JIJ5; -.
DR STRING; 391038.Bphy_2869; -.
DR KEGG; bph:Bphy_2869; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_4; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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:ACC72041.1};
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:ACC72041.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Transferase {ECO:0000313|EMBL:ACC72041.1}.
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 761 AA; 81609 MW; FAF6DD12E7F092A1 CRC64;
MDEQLKQSAL AYHQNPKPGK ISVTPTKPLS NQLDLSLAYS PGVAAACMAI YDEPLDAQKY
TSRGNLVGVI TNGTAVLGLG NIGPLAAKPV MEGKGCLFKK FAGIDVFDIE LSESDPDKLV
EAIAMLEPTL GGINLEDIKA PECFYIEKKL RERMKIPVFH DDQHGTAIIA SAAILNGLKV
VGKKLEDIKL VCSGAGAAAI ACLDLLVHLG LKKSNTLVVD SKGVIYEGRG NLDASKERYQ
ASTDARTLGD AMHGCDVFLG CSSAGVLKPE MVTTMADKPL ILALANPEPE IRPEEAKKVR
PDAIIATGRS DYPNQVNNVL CFPFIFRGAL DVGATTITEE MKLACVRAIA ELAEETDQGD
EVAKAYEGHS LEFGPDYLIP KPFDPRLIIK IAPAVAQAAM DSGVATRPIQ DMDAYREQLG
ATVYRTGMVM RPVFAAAKAQ PARIVFAEGE DERVLRAAQF VLLEKIAKPI LVGRPSVIEM
RLKKMGSKLK CGEDVEIVNP EDDPRYQKSW QAYHEIGARE GVTPEVAKAA MRKFNTLIGA
ILVHLGDADG MICGLIDTYH EHLKFVEQVL GKAANVDNFA AMNLLMLPGR NLFISDTYVN
EVPTAEQLAD MTILAAREIE KFGIVPKVAL LSNSNFGSIP SSSAARMAQA RKLIAARAPH
LEVDGEMHGD AALSEAVRKA AFPGTTLTGE ANLLIMPNVE AANITYNLLK MIGGEGVTVG
PFLLGAAKPV HILTPAATVR RIINMTAVAS ANASVDRQAA K
//
