ID A0A1X1DCE2_9GAMM Unreviewed; 759 AA.
AC A0A1X1DCE2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:ORM74366.1};
GN ORFNames=HA48_04670 {ECO:0000313|EMBL:ORM74366.1};
OS Pantoea wallisii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1076551 {ECO:0000313|EMBL:ORM74366.1, ECO:0000313|Proteomes:UP000193104};
RN [1] {ECO:0000313|EMBL:ORM74366.1, ECO:0000313|Proteomes:UP000193104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26277 {ECO:0000313|EMBL:ORM74366.1,
RC ECO:0000313|Proteomes:UP000193104};
RX PubMed=28255640;
RA Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT "Phylogenomic resolution of the bacterial genus Pantoea and its
RT relationship with Erwinia and Tatumella.";
RL Antonie Van Leeuwenhoek 0:0-0(2017).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:ORM74366.1}.
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DR EMBL; MLFS01000008; ORM74366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1DCE2; -.
DR STRING; 1076551.HA48_04670; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000193104; 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; IPR015884; Malic_enzyme_CS.
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.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW 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}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..401
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 288
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 759 AA; 81966 MW; 3CEDD486AB52907E CRC64;
MDDQLKQSAL DFHQYPTPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI AADPLAAHKY
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGIDVFDIE IDEHDPDKLI
EVIAALEPTF GGINLEDIKA PECFYIEQKL RERMQIPVFH DDQHGTAIIC TAAVLNGLQV
VGKSIAEVRL VVSGAGASAI ACLNLLVALG LQQHNIVVCD SKGVIYRDRE PDMAPTKAAY
AVADSGARTL DDVMGGADIF LGCSGPKALT PGMVQKMAQD PLILALANPE PEIMPPLAKQ
VRPDAIICTG RSDFPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVHA IAALAQAEQS
DVVASAYDDQ DLSFGAEYLI PKPFDPRLIV QIAPAVAQAA MESGVATRPI EDFEAYREQL
TEFVYKTNLF MKPIFSQARK APKRVVLAEG EEVRVLHATQ ELVSLGLAKP ILIGRPNVIA
MRLQKQGLKI EAGKDFEIVN NESDPRFKAY WNEYYQLMKR RGVTPETAQR AVIGNPTLIG
AIMVHRGEAD AMICGTIGDY REHYDVVERV FGFRDDVKVA GAMNALLLPS GNTFIADTYV
NEDPSAQQLA DITLLAAETV RRFGIEPRVA LLSHSSFGTS NAPGARKMRE ALALIQQRAP
DLEVDGEMHG DAALVESIRR EQMPDSPLKG TANLLIMPNV EAARISYNLL RVSCSEGVTV
GPVLMGIRKP VHVLTRIASV RRIVNMVALA VVEAQTEPL
//
