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Database: UniProt
Entry: S3Z892_9ACTN
LinkDB: S3Z892_9ACTN
Original site: S3Z892_9ACTN 
ID   S3Z892_9ACTN            Unreviewed;       413 AA.
AC   S3Z892;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative NAD-dependent malic enzyme {ECO:0000313|EMBL:EPH39378.1};
GN   ORFNames=STRAU_7579 {ECO:0000313|EMBL:EPH39378.1};
OS   Streptomyces aurantiacus JA 4570.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH39378.1, ECO:0000313|Proteomes:UP000014629};
RN   [1] {ECO:0000313|EMBL:EPH39378.1, ECO:0000313|Proteomes:UP000014629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA 4570 {ECO:0000313|EMBL:EPH39378.1,
RC   ECO:0000313|Proteomes:UP000014629};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT   Setomimycin.";
RL   Submitted (FEB-2013) 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}.
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:EPH39378.1}.
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DR   EMBL; AOPZ01000542; EPH39378.1; -; Genomic_DNA.
DR   RefSeq; WP_016645685.1; NZ_AOPZ01000542.1.
DR   AlphaFoldDB; S3Z892; -.
DR   PATRIC; fig|1286094.4.peg.7507; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000014629; 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   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; 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:UP000014629}.
FT   DOMAIN          41..174
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          186..406
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        117
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         160
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         185
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   413 AA;  42718 MW;  5787C4A8CFEB35E1 CRC64;
     MAAEIVNPRS DSSGSRGTSG STAGHEGTEE PFDPAFALHR GGKMAVQATV PVRDKDDLSL
     AYTPGVAKVC SAIAEQPELV HDYTWKSNVV AVVTDGTAVL GLGDIGPEAS LPVMEGKAIL
     FKQFGGVDAV PIALATTDVD EIIDTVVRLA PSFGGVNLED ISAPRCFEIE RRLQERLDIP
     VFHDDQHGTA VVTLAALRNA ARLTGRTLGD LRAVISGAGA AGVAIAKFLL EAGLGDVAVA
     DRKGVVSRDR DDLTPVKREL AELTNKAGLS GSLESALDGA DVFIGVSGGT VPEPAVASMA
     PNSFVFAMAN PNPEVHPDIA HKYASVVATG RSDYPNQINN VLAFPGIFAG ALQVRASRIT
     EGMKIAAADA LADVVGDELS ADYVIPSPFD ERVAPAVTAA VAAAARAEGV ARR
//
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