ID C9XWX4_CROTZ Unreviewed; 592 AA.
AC C9XWX4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=NAD-dependent malic enzyme {ECO:0000256|HAMAP-Rule:MF_01619};
DE Short=NAD-ME {ECO:0000256|HAMAP-Rule:MF_01619};
DE EC=1.1.1.38 {ECO:0000256|HAMAP-Rule:MF_01619};
GN Name=sfcA {ECO:0000313|EMBL:CBA28359.1};
GN Synonyms=maeA {ECO:0000256|HAMAP-Rule:MF_01619};
GN OrderedLocusNames=Ctu_08890 {ECO:0000313|EMBL:CBA28359.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA28359.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.38; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01619};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01619}.
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|RuleBase:RU003427}.
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DR EMBL; FN543093; CBA28359.1; -; Genomic_DNA.
DR AlphaFoldDB; C9XWX4; -.
DR KEGG; ctu:CTU_08890; -.
DR PATRIC; fig|693216.3.peg.850; -.
DR HOGENOM; CLU_011405_5_2_6; -.
DR Proteomes; UP000002069; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd05312; NAD_bind_1_malic_enz; 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 HAMAP; MF_01619; NAD_malic_enz; 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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR023667; NAD_malic_enz_proteobac.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 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, ECO:0000256|HAMAP-
KW Rule:MF_01619};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01619};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01619}.
FT DOMAIN 107..287
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 297..558
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 445
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT SITE 296
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
SQ SEQUENCE 592 AA; 65898 MW; A23753EE260541AF CRC64;
MVIRPFRRGL QKANGEASAA QKRVRQMEIK HKKNRSLYIP YAGPVLLEFP LLNKGSAFSM
EERSNFNLLG LLPEVVETIE EQAERAWRQF EDFKTDIDKH IYLRNIQDTN ETLFYRLLEN
HLEVMMPIIY TPTVGSACER FSEIYRRARG VFISWPNRHN MDDILQNVPI HNIKVIVVTD
GERILGLGDQ GIGGMGIPIG KLSLYTACGG ISPAYTLPIV LDAGTNNQQL LNDPLYMGWR
HPRITDDEYY AFVDDFIQAV KQRWPNVLLQ FEDFAQKNAM PLLERYRDEI CCFNDDIQGT
AAVTLGTLIA ASRAAGSQLS EQKIVFLGAG SAGCGIAEQI IAWMRTEGGL SDEQARARVY
MVDRFGLLTD NMPNLLSFQS KLVQKRDSLQ GWDTQSDSIS LLDVVRNAKP DILIGVSGQT
GLFTEEIIRE MHKHCARPIV MPLSNPTSRV EATPHDILNW TDGAALVATG SPFQPVTVKE
KTYPIAQCNN AYIFPGIGLG IISSGALRVT DEMMMAASEA LASHSPLVNT GSGLVLPPLT
DIQAVSKDIA FAVGKMAQQQ GVAVKTSAEA LLQAIEDNFW LPEYRSYRRT SI
//
