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Database: UniProt
Entry: A0A0K2ATA4_STRA7
LinkDB: A0A0K2ATA4_STRA7
Original site: A0A0K2ATA4_STRA7 
ID   A0A0K2ATA4_STRA7        Unreviewed;       471 AA.
AC   A0A0K2ATA4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:AKZ56037.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:AKZ56037.1};
GN   ORFNames=SAM23877_2988 {ECO:0000313|EMBL:AKZ56037.1};
OS   Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS   NBRC 12836 / NRRL B-2516).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=278992 {ECO:0000313|EMBL:AKZ56037.1, ECO:0000313|Proteomes:UP000061018};
RN   [1] {ECO:0000313|Proteomes:UP000061018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL
RC   B-2516 {ECO:0000313|Proteomes:UP000061018};
RX   PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA   Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA   Leblond P.;
RT   "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT   spiramycin producer.";
RL   J. Biotechnol. 214:117-118(2015).
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; CP012382; AKZ56037.1; -; Genomic_DNA.
DR   RefSeq; WP_053131825.1; NZ_CP012382.1.
DR   AlphaFoldDB; A0A0K2ATA4; -.
DR   STRING; 1889.SAM40697_2735; -.
DR   KEGG; samb:SAM23877_2988; -.
DR   Proteomes; UP000061018; 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   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; IPR002912; ACT_dom.
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.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Oxidoreductase {ECO:0000313|EMBL:AKZ56037.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061018}.
FT   DOMAIN          12..86
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   471 AA;  48717 MW;  A63AB9F1A8382050 CRC64;
     MATAPSVSYS MTVRLEVPAG GTAVSQLTTA VESAGGSVTG LDVTASGHDK LRIDVTIAAG
     STSHADEIVE QLRGIEGVSL GKVSDRTFLM HLGGKIEMAS KHPIRNRDDL SMIYTPGVAR
     VCMAIAENPE DARRLTIKRN SVAVVTDGSA VLGLGNIGPK AALPVMEGKA ALFKRFAGID
     AWPLCLDTQD TDAIVEIVKA IAPGFAGINL EDISAPRCFE IEARLREALD IPVFHDDQHG
     TAIVVLAALT NALRVVDKPI ENVRVVMSGA GAAGTAILKL LLAAGVKNAV VADIHGVVHA
     GRADLVDAAP ESALRWIADN TNPEGLTGTL KEAVHGADVF IGVSAPNVLD GEDVAAMADG
     AIVFALANPD PEVDPAIARQ TAAVVATGRS DFPNQINNVL VFPGVFRGLL DAQSRTVNTE
     MMLAAAHALA DVVTEDEINP NYIIPSVFND KVAGAVAGAV REAAKAAGVV A
//
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