ID Q215P6_RHOPB Unreviewed; 769 AA.
AC Q215P6;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate decarboxylating) (NADP+)., Phosphate acetyltransferase {ECO:0000313|EMBL:ABD87890.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ABD87890.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:ABD87890.1};
GN OrderedLocusNames=RPC_2337 {ECO:0000313|EMBL:ABD87890.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD87890.1};
RN [1] {ECO:0000313|EMBL:ABD87890.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD87890.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000301; ABD87890.1; -; Genomic_DNA.
DR AlphaFoldDB; Q215P6; -.
DR STRING; 316056.RPC_2337; -.
DR KEGG; rpc:RPC_2337; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
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:ABD87890.1};
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:ABD87890.1}; Transferase {ECO:0000313|EMBL:ABD87890.1}.
FT DOMAIN 21..154
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 166..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 79..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 769 AA; 82574 MW; 22B6ADE3CD6ABE2E CRC64;
MATNSEELQA AALAYHRLPR PGKLEIKAIK PLANQLDLAL AYTPGVAAAC NAIAADPTQA
ASLTIRGNLV AVVTNGTAVL GLGNIGPLAS KPVMEGKAVL FKKFADIDVF DIEIAADTVE
RVVETVAALE PTFGGINLED IKGPECFEIE AQLKDRMKIP VFHDDQHGTA IIVGAAVKNA
LQLTGKKLDE VKIVAAGAGA AALACLNLLV LLGAQRKNIW VCDLEGLVYE GREKLMDRWK
AVYAQPTDKR VLAEVIGGAD IFLGLSGPKV LTPEMVAQMA ERPLVMALAN PTPEIMPDEV
RKVRPDAMIC TGRSDFPNQV NNVLCFPYIF RGALDVGATA INEEMKAAAV DAIALLARDP
PSEAMTIGFD GDEELGFGPG SLIPSPFDPR LILRIAPAVA KAAMDSGVAT RPITDFDEYS
AQLERFAFRS GLVMKPLFTK AKAQPVRVIY AEGEDERVLH ATQTILEEKL ARPILVGRPA
VVAARIKRYG LSIRAGQDFD LINPEDDPRY RSYVQSYIDV AGRRGVTPET ARTMVRTNAT
VIAALAVARG EADAMICGVD GRYMSHLRHV REIIGSLPGI TDFAALSLMI TSKGAIFIAD
TQVRPNPSAE ELAEIAALAA IHVQRFNMKP RIAFVSHSDF GSYDTESSRK MRRATAILAE
NHPEIEADGE MHGDTALSEA ARKFILPHSR LEGQANVLIM PNLDTANVAY QMIKVLADAL
PVGPILIGPA RPAHILTPSV TSRGILNMTA VAAVEAQERA GRQQPTLFA
//
