ID A0A2W7N5D8_9RHOB Unreviewed; 759 AA.
AC A0A2W7N5D8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:PZX15258.1};
GN ORFNames=LX81_02561 {ECO:0000313|EMBL:PZX15258.1};
OS Palleronia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=568105 {ECO:0000313|EMBL:PZX15258.1, ECO:0000313|Proteomes:UP000248916};
RN [1] {ECO:0000313|EMBL:PZX15258.1, ECO:0000313|Proteomes:UP000248916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22009 {ECO:0000313|EMBL:PZX15258.1,
RC ECO:0000313|Proteomes:UP000248916};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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:PZX15258.1}.
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DR EMBL; QKZL01000010; PZX15258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7N5D8; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000248916; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000248916}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 759 AA; 81824 MW; ED2395056350D2C0 CRC64;
MDEERKAALR AAALDYHRYP KPGKLEIRAT KPMANGRDLA RAYSPGVAEA CLEIKDDPEA
ARDYTARGNL VAVVSNGTAV LGLGNIGALA SKPVMEGKAV LFKKFANIDC FDIEIDETDP
EKLAAIVCAL EPSFGAINLE DIKAPDCFTV ERICREKMNI PVFHDDQHGT AIVVGAAATN
ALRVAKKTFE ELKIVSTGGG AAGIACLDML LKLGVKRENV WLCDIHGLVH EGREEDMNPQ
KAAYAQPGGA RSLGEVIDGA DLFLGLSGPG VLKPEMVAKM AENPIIFALA NPNPEIDPTE
AREVAPGALI ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT TINDEMKIAC IEGIAALARI
TTSAEAAAAY KGEQMSFGPD YLIPKPFDPR LMGIVASAVA KAAMESGVAA RPIEDLAAYK
RKLDGSVFKS ALIMRPVFDA AAKNARRIVF AEGEDERVLR AANAMLEETT DKPILIGRPE
VVEQRAERAG LTIRPGRDFD LVNPENDPRY RDYWGTYHEI MQRRGVTPDI AKAIMRTNST
AIGAVMVHRD EADSMICGTF GQYLWHLNYV HQVLGTKDLY PVGALSLMIL EDGPLFIADT
HVHPSPSPQQ IAETVIGAAR HVRRFGIVPQ IALCSHSQFG NFDCDTGLRM RAALEILDQE
ERSFCYEGEM HADAALDPEL RARIFPNSRM AGAANVLVFA NTDAASGVRN ILKMKAGGLE
VGPILMGMAN RAHIVTSSIT ARGLLNVSAI AGTPVAEYS
//
