ID C5TAN0_ACIDE Unreviewed; 756 AA.
AC C5TAN0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+))., Phosphate acetyltransferase {ECO:0000313|EMBL:EER58465.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EER58465.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:EER58465.1};
DE Flags: Fragment;
GN ORFNames=AcdelDRAFT_3960 {ECO:0000313|EMBL:EER58465.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER58465.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER58465.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER58465.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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:EER58465.1}.
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DR EMBL; ACQT01000260; EER58465.1; -; Genomic_DNA.
DR RefSeq; WP_005799688.1; NZ_ACQT01000260.1.
DR AlphaFoldDB; C5TAN0; -.
DR PATRIC; fig|573060.9.peg.998; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000003856; 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:EER58465.1};
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:EER58465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW Transferase {ECO:0000313|EMBL:EER58465.1}.
FT DOMAIN 25..158
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 170..407
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 83..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT NON_TER 756
FT /evidence="ECO:0000313|EMBL:EER58465.1"
SQ SEQUENCE 756 AA; 81249 MW; F0CD8D6E6CB3E6B0 CRC64;
MTQKLSAAEE SLRDAARDYH RNITRGKISV TPTKPLSNQR DLSLAYSPGV AYPCLDIQAD
PTKAFDYTSR GNLVGVITNG TAVLGLGDIG PLAGKPVMEG KGCLFKKFAG VDVFDIELAE
RDPDKLIDII ASLEPTLGGI NLEDIKAPEC FYIERELSKR MNIPVFHDDQ HGTAIISSAA
LLNGLELVGK QIDQVKIAVS GAGAAAIACV GVMVGLGVKV ENIFMCDSKG VIYEGRPGGY
DESKARYAQK TDARTLADAV HGADVFLGCS APGVLTAEMV KTMAPKPIIL ALANPEPEIR
PELAKAVRPD CIIATGRSDY PNQVNNVLCF PYIFRGALDC GATKITEAMK LACVRQIADL
AKADISEEVA SAYAGKELTF GPDYLIPTPF DSRLILKIAP AVAKAAAESG VATRPIADME
AYKETLSRFV YQTGMLMRPV INAAKALPDA QKRVAYADGE DERALRAAQM AIDDKIAQPI
LIGRPAVIAA RIAKAGLRMQ LGKDVEVCNP EDDPRFRQYW ERYHQLMKRD GATPEVAKAA
VRRSNTIIAS LMVSLGDADA MICGLVGTYE THLDRIHSIL GRQPGVNDYA ALNALMTNRG
TLFIADTYVN EDPTAQQLAD IAWMSVQEVQ RFGLPAKVAF LSHSSYGSSK RASAKKMRLA
RDLFVAAHPD IECDGELHGD AALEPNIRNA YMADSTLTDS ANLLICPNID AANILYNVLK
TTTSGGVTVG PILMGVAATA YILTPAATVR RVFNMT
//
