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Database: UniProt
Entry: G5LNW6_SALET
LinkDB: G5LNW6_SALET
Original site: G5LNW6_SALET 
ID   G5LNW6_SALET            Unreviewed;       277 AA.
AC   G5LNW6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:EHC39436.1};
DE   Flags: Fragment;
GN   ORFNames=LTSEALA_2386 {ECO:0000313|EMBL:EHC39436.1};
OS   Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC39436.1, ECO:0000313|Proteomes:UP000004642};
RN   [1] {ECO:0000313|EMBL:EHC39436.1, ECO:0000313|Proteomes:UP000004642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R6-377 {ECO:0000313|EMBL:EHC39436.1,
RC   ECO:0000313|Proteomes:UP000004642};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|RuleBase:RU003427}.
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:EHC39436.1}.
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DR   EMBL; AFCJ01001033; EHC39436.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5LNW6; -.
DR   PATRIC; fig|913241.3.peg.1803; -.
DR   Proteomes; UP000004642; Unassembled WGS sequence.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU003427}.
FT   DOMAIN          1..243
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHC39436.1"
SQ   SEQUENCE   277 AA;  30199 MW;  A8D844B940653066 CRC64;
     AGSQLSEQKI VFLGAGSAGC GIAEQIIAQT QREGLSEDAA RQNVFMVDRF GLLTDRMPNL
     LPFQAKLVQK CDNLQHWDTE NDVLSLLDVV RNVKPDILIG VSGQTGLFTE EIIREMHKHC
     PRPIVMPLSN PTSRVEATPQ DIIAWTEGNA LVATGSPFSP VIWKDKVYPI AQCNNAYIFP
     GIGLGVIASG ASRITDEMLM SASETLAKHS PLVNNGEGLV LPALKDIQVV SRAIAFAVGK
     MAQQQGVAVK TSAEALQQAI DDNFWKPEYR DYRRTSI
//
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