ID F6IEW1_9SPHN Unreviewed; 760 AA.
AC F6IEW1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:CCA90836.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:CCA90836.1};
GN ORFNames=PP1Y_Mpl10035 {ECO:0000313|EMBL:CCA90836.1};
OS Novosphingobium sp. PP1Y.
OG Plasmid Mpl {ECO:0000313|EMBL:CCA90836.1,
OG ECO:0000313|Proteomes:UP000009242}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA90836.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA90836.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RC PLASMID=Mpl {ECO:0000313|EMBL:CCA90836.1,
RC ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
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}.
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DR EMBL; FR856861; CCA90836.1; -; Genomic_DNA.
DR RefSeq; WP_013837075.1; NC_015583.1.
DR AlphaFoldDB; F6IEW1; -.
DR KEGG; npp:PP1Y_Mpl10035; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000009242; Plasmid Mpl.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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: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 ECO:0000313|EMBL:CCA90836.1}; Plasmid {ECO:0000313|EMBL:CCA90836.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009242}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..399
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 760 AA; 81835 MW; CB930B70838453BD CRC64;
MDENLRKAAL EYHLFPQPGK LRIEPTKRMV NQRDLALAYS PGVAAPCEEI AADPDKAADY
TARGNLVAVI SNGTAVLGLG AIGALASKPV MEGKAVLFKK FADIDVFDIE VDTTDPDRFV
DAVSLLEPTF GGINLEDIKA PECFAIEAAL RERMNIPVFH DDQHGTAIVV AAAVRNALVL
QGKSLGEAKL VTSGAGAAAL ACVDLLVSMG LPAENVTLTD KDGVIHAGRE GMLPNMARYA
RQTDARTLPE VLPGANVFLG LSAPGVLKPE WLPLLADKPL IFALANPEPE ILPDIARASR
PDAIIATGRS DFPNQVNNVL CFPYIFRGAL DVGATTINEE MKVAAAEAIA SLARLPAHES
VAQAYGGRKL AFGPEYIIPT PFDPRLIAEI APAVAKAAMD SGVARRPLDL EVYRRSLAQK
NTRSAQLMMP VFEAARGSQT RIAYGEGEDE RVLRAVQDVL DDGIARPVIV ARRRILERRL
PELGLRFELD RDVEVIDPET DHAIIEPLVE AYRNVAGRKG VPAPEIVRHI YRRPTVTAAM
LLRTGQVDAA LVGGNSEYWG QMEYVLRIID RAPGAQRVYA LSGLILDAGA LFITDTHMVP
EPTPEQIAEM TLLASREIRH FGLEPRVALL SHSNFGASHS PSARKMRAAL AMLREKAPDL
AVDGEMHADA ALSQPLRERL VPDTRFEGPA NLLVMPNLDA ANITLTALGA SSSSPTVGPM
LMGLSRPIHV MTPSMTSRSV LNMTTIAVSE AMNRDRAKGA
//
