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Database: UniProt
Entry: D7BW78_STRBB
LinkDB: D7BW78_STRBB
Original site: D7BW78_STRBB 
ID   D7BW78_STRBB            Unreviewed;       559 AA.
AC   D7BW78;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ADI11788.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:ADI11788.1};
GN   OrderedLocusNames=SBI_08670 {ECO:0000313|EMBL:ADI11788.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11788.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI11788.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11788.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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, ECO:0000256|RuleBase:RU003427}.
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DR   EMBL; CP002047; ADI11788.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7BW78; -.
DR   STRING; 749414.SBI_08670; -.
DR   KEGG; sbh:SBI_08670; -.
DR   PATRIC; fig|749414.3.peg.8919; -.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_011405_5_2_11; -.
DR   OMA; ANYDTAN; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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   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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:ADI11788.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          80..262
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          272..531
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         248
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         271
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   559 AA;  60440 MW;  3FEAF84718ABECE9 CRC64;
     MDQTMPHSPQ PTSSPGATIL ANPLANKGTA FTRSERSELG LDGLLPPAVE TLDEQVARAY
     EAFRGYDKPL NRHIYLRQLQ DTNEVLFHRL VTDHLEELLP VVYTPTVGEA CQRFSEIYRR
     PRGLFLTWED RHRFGEILRN RPHRDQDVDV IVVTDGQRIL GLGDQGVGGM GIPIGKLSLY
     TAIGGIHPAR TLPVLLDVGT DNEELLDNPR YLGRRARRLT GAEYDEMVEA FVSAVETELP
     GSLLQWEDFA TAHARPILTR YRDRLLTFND DIQGTAAVAL GALSTAADVA GTPLSEQRLV
     LLGAGSAAIG VADMIRTAMI EEGLTEAEAA AHFWIVDVNG LLVRSRTDLT EEQRVYARED
     SEVTDWASTS LAEVVRRVAP TALIGLSTAH GAFTEEIVRQ MASACARPVI FPLSNPTSHA
     EADPADLTRW TDGRALIATG SPFPPLTVDG REVPVAQSNN VYVFPAIGLA VTASQATRVT
     DRMLVAAAHA VAQCAVRSAD GADGPVPLLP PLSGMPEAAR EIALAAALAA VEDQVAPKAS
     EDALREAIAA AQWTPRYEV
//
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