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Database: UniProt
Entry: M7AB93_9ACTN
LinkDB: M7AB93_9ACTN
Original site: M7AB93_9ACTN 
ID   M7AB93_9ACTN            Unreviewed;       411 AA.
AC   M7AB93;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 2.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EMP11290.2};
GN   ORFNames=ISGA_2887 {ECO:0000313|EMBL:EMP11290.2};
OS   Gordonia sp. NB41Y.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP11290.2, ECO:0000313|Proteomes:UP000011989};
RN   [1] {ECO:0000313|EMBL:EMP11290.2, ECO:0000313|Proteomes:UP000011989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP11290.2,
RC   ECO:0000313|Proteomes:UP000011989};
RX   PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA   Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT   "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT   to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL   Microbiology 159:1618-1628(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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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:EMP11290.2}.
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DR   EMBL; APHK02000067; EMP11290.2; -; Genomic_DNA.
DR   AlphaFoldDB; M7AB93; -.
DR   STRING; 1241906.ISGA_2887; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000011989; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_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   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   PIRSF; PIRSF000106; ME; 1.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011989}.
FT   DOMAIN          40..173
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          185..405
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         158
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         184
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   411 AA;  42823 MW;  C57D9F70736A933B CRC64;
     MRRKTVTSTE NNVTQDEGLV EPAIADQPIT DEEIFMAHAG GKLSVELRSP IETQRDLSIA
     YTPGVAQVSR AIHGESALVD KYTWTDRLVA VVSDGSAVLG LGDIGPRASL PVMEGKSALF
     RTFAGLNSIP IVLDTKDPDE IVETLIRLRP SFGAVNLEDI SAPRCFEIER RVIEALDCPV
     MHDDQHGTAI VVLAALKGAV RLLERDLASL RVVISGAGAA GVACANILLA AGVSDVVVLD
     SKGIVSTGRE GLNEFKDDLA ARTNPRGLVG GAAVALDGAD VFLGVSAGKI DESLIASMNE
     GSIVFALSNP DPEIHPEVAA KYAAIVATGR SDFPNQINNV LAFPGVFKGA LDAGARRITE
     SMKIAAAEAI LSVVADELAA DKIVPSPLDQ RVAPAVAQAV AAVAEAEGLC S
//
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