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Database: UniProt
Entry: A0A1H1AMN7_9ACTN
LinkDB: A0A1H1AMN7_9ACTN
Original site: A0A1H1AMN7_9ACTN 
ID   A0A1H1AMN7_9ACTN        Unreviewed;       398 AA.
AC   A0A1H1AMN7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:SDQ40939.1};
GN   ORFNames=SAMN04489764_0567 {ECO:0000313|EMBL:SDQ40939.1};
OS   Thermostaphylospora chromogena.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermostaphylospora.
OX   NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ40939.1, ECO:0000313|Proteomes:UP000217103};
RN   [1] {ECO:0000313|EMBL:SDQ40939.1, ECO:0000313|Proteomes:UP000217103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ40939.1,
RC   ECO:0000313|Proteomes:UP000217103};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNKK01000002; SDQ40939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1AMN7; -.
DR   STRING; 35622.SAMN04489764_0567; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000217103; 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   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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217103}.
FT   DOMAIN          26..159
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          171..391
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        47
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         144
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         145
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   398 AA;  41357 MW;  BE57ADB20282C8DB CRC64;
     MAISPSSTAS TGDAIDTDPA FALHRGGKLE VRSTVPVRDA DDLSLAYTPG VARVCTAIAD
     TPELVKDYTW VSRVVAVVSD GTAVLGLGDI GPSAAMPVME GKALLFKEFA GVDAVPICLD
     CTDVDELVET VVRLAPSFGG INLEDISAPR CFEVEDRLRE RLDIPVFHDD QHGTAIVVLA
     ALRNAARLTG RSLGDLRAVV AGAGASGVAV TRILQSAGIG DIAVSDSKGV IYPGREGLNP
     VKRALAEETN RARLTGSTEE ALAGADVFIG LSGSTIAEEA LASMADDAIV FALSNPTPEV
     HPDVARRHAR VVATGRSDFP NQINNVLAFP GVFRGALDVR ARTITEGMKT AAAMALADVV
     GDRLCADYVI PSPFDPRVAP AVSAAVAARA REEGVARA
//
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