ID K8A062_9ENTR Unreviewed; 759 AA.
AC K8A062;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:CCJ72608.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:CCJ72608.1};
GN ORFNames=BN137_1976 {ECO:0000313|EMBL:CCJ72608.1};
OS Cronobacter condimenti 1330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1073999 {ECO:0000313|EMBL:CCJ72608.1, ECO:0000313|Proteomes:UP000009340};
RN [1] {ECO:0000313|EMBL:CCJ72608.1, ECO:0000313|Proteomes:UP000009340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330 {ECO:0000313|EMBL:CCJ72608.1,
RC ECO:0000313|Proteomes:UP000009340};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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:CCJ72608.1}.
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DR EMBL; CAKW01000071; CCJ72608.1; -; Genomic_DNA.
DR RefSeq; WP_007672198.1; NZ_CP012264.1.
DR AlphaFoldDB; K8A062; -.
DR STRING; 1073999.AFK62_14510; -.
DR KEGG; ccon:AFK62_14510; -.
DR PATRIC; fig|1073999.7.peg.3043; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000009340; 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:CCJ72608.1}.
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; 82266 MW; 4E69F4011D80F5F4 CRC64;
MDEQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI AADPLAAYKY
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGIDVFDIE IDEHDPDKVV
DVVAALEPTF GGINLEDIKA PECFYIEKKL RERMNIPVFH DDQHGTAIIC TAAVLNGLRV
VQKNISDVRL VVSGAGASAI ACMNLLVALG MQKRNIVVCD SKGVIYKGRE ENMAETKAAY
AIDDNGKRTL GEVIEGADIF LGCSGPKVLT QEMVKLMADS PLILALANPE PEIMPPLAKA
VRPDAIICTG RSDFPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVHA IAQLAHAEQS
EVVASAYEDQ ELSFGPDYII PKPFDPRLIV TIAPAVAKAA MESGVATRPI EDFDAYKDKL
TEFVYKTNLF MKPVFNQARK DPKRVVLTEG EEPRVLHATQ ELITLGLAKP VLIGRPGVIE
MRLKKLGLQM EAGKDFEIVN NESDPRYKEY WNEYYSIMKR RGVTQEQAQR AVIGNSTVIG
AIMVHRGEVD AMICGTIGDY HEHFSVVQQI FGYRDGVKAA GAMNALLLPS GNTFIADTYV
NDDPTPEQLA EITVMAAETV RRFGIEPKVA LLSHSHFGSS DSPAASKMRE TLQLVRERVP
ELMIDGEMHG DAALVESIRN DRMPDSPLKG SANVLIMPNV EAARISYNLL RVSSSEGVTV
GPVLMGVAKP VHVLTPIASV RRIVNMVALA VVEAQTNPL
//
