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Database: UniProt
Entry: M5J7N3_9LACO
LinkDB: M5J7N3_9LACO
Original site: M5J7N3_9LACO 
ID   M5J7N3_9LACO            Unreviewed;       540 AA.
AC   M5J7N3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EKW99812.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:EKW99812.1};
GN   ORFNames=D271_00250 {ECO:0000313|EMBL:EKW99812.1};
OS   Ligilactobacillus saerimneri 30a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99812.1, ECO:0000313|Proteomes:UP000011912};
RN   [1] {ECO:0000313|EMBL:EKW99812.1, ECO:0000313|Proteomes:UP000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:EKW99812.1,
RC   ECO:0000313|Proteomes:UP000011912};
RX   PubMed=23405290;
RA   Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA   Lolkema J.S., Lucas P.M.;
RT   "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT   sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT   Biogenic Amines.";
RL   Genome Announc. 1:E00097-E00012(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, 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:EKW99812.1}.
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DR   EMBL; ANAG01000001; EKW99812.1; -; Genomic_DNA.
DR   RefSeq; WP_009550788.1; NZ_ANAG01000001.1.
DR   AlphaFoldDB; M5J7N3; -.
DR   STRING; 1227363.D271_00250; -.
DR   GeneID; 80985967; -.
DR   PATRIC; fig|1227363.6.peg.49; -.
DR   Proteomes; UP000011912; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043883; F:malolactic 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:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043464; P:malolactic fermentation; IEA:InterPro.
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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR048182; Malolactic_enz.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF041582; malolactic; 1.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF34; 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,
KW   ECO:0000256|PIRSR:PIRSR000106-3}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:EKW99812.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011912}.
FT   DOMAIN          68..250
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          260..516
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         235
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         236
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         259
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         448
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   540 AA;  59233 MW;  4B33A9C06D529EB3 CRC64;
     MPQAATILNN PYLNKGTGFT YEERKELGLV GALPPRVQTL AEQAEQAYQQ FQRIEDGLDQ
     RLFLMKIFDT NRTLFYYLFG QHIVEFMPIV YDPVIAESIE QYSEIYTRPQ DAAFISIDRM
     DEIEDTLRNA ASGRDIRLIV VTDGEGILGI GDWGVNGVDI SVGKLMVYTA AAGIDPAQVL
     AVSLDAGTNN EQLLADPLYL GNRHERVYGD RYYEMVDKFV AAAEKLFPQV LLHFEDFGRA
     NASNILNKYQ DKILTFNDDI QGTGIICLAG VLGALNISKQ KITDQTFLTF GAGNAGVGIA
     KMMYDELLRE GLTPEEAKQH FYLVDKQGLL FEDTPDLTPE QKQFLRKRSE FANADELTNL
     EAVVKAVHPT VMIGTSKQPG AFTEVIVKEM AAHTERPIIF PISNPTKLAE AKAADLLKWT
     DGKALIGTGI PVAPIEYKGV TYEIGQANNA LVYPGVGVGA LAVNAKVINE KMLAQAAHAL
     GGIVDPDQPG AAVLPPVERL TEFSTTVAET VAQSAIDQGL AQTDLTVHDA VQAMKWEPKY
//
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