ID A0A0J5FR49_9GAMM Unreviewed; 759 AA.
AC A0A0J5FR49;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KMJ44743.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KMJ44743.1};
GN ORFNames=AB204_12720 {ECO:0000313|EMBL:KMJ44743.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ44743.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ44743.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ44743.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMJ44743.1}.
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DR EMBL; LFCV01000080; KMJ44743.1; -; Genomic_DNA.
DR RefSeq; WP_047963738.1; NZ_LFCV01000080.1.
DR AlphaFoldDB; A0A0J5FR49; -.
DR STRING; 880157.AB204_12720; -.
DR PATRIC; fig|880157.4.peg.2719; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000036277; Unassembled WGS sequence.
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; 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,
KW ECO:0000313|EMBL:KMJ44743.1}.
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; 82530 MW; 4856FAA2FD60A1F3 CRC64;
MDEKLKQSAL DFHEFPQPGK ITVTPTKPLT TQRDLALAYS PGVAAPCLEI AEDPLAAYKY
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FSGIDVFDIE VDESNPDKLI
DIIAALEPTF GGINLEDIKA PECFYIEQKL RERMKIPVFH DDQHGTAIIC TAAVLNGLRV
VSKDISTVRM VVSGAGAASI ACMNLLVALG LKRENIVVCD SKGVIYRGRE ENMEKTKADY
AIEDNGSRTL ADVIPDADIF LGCSGPGVLT QDMVKTMAKD PLIMALANPE PEILPPLAKA
VRPDAIICTG RSDFPNQVNN VLCFPFIFRG ALDVGATTIN EEMKLACVRA IADLALAEQS
QEVASAYGDQ DLFFGPDYII PKPFDPRLIV KIAPAVAKAA MESGVATRPI TDFGAYIEKL
NEFVYKTNLF MKPIFSQAKK EKKRIVLAEG EDIRVLHATQ ELVSLGLAFP ILIGRPSVIE
MRIKKQGLHI EAGKDFEVVN NENDPRFKEY WQEYYQLMKR RGVSQEQARR AVIGDPTLIG
AIMVHRGEAD GLICGTVGSY SEHYQVVKDV FGFRQGVHTA GAMNALMLPT GNTFIADTYV
NEDPNPEELA EITLMAAETI RRFGIEPKVA LLSRSSFGSA DCDSAQKMRK TLELVQKMAP
SLEIDGEMHG DAALMESIRR DIMPDSPLKG SANLLIMPNM EAARISYNLL RVTSSDGVTV
GPVLMGVAKP IHILTPIASV RRIVNMVALA AVEAQTNPL
//
