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Database: UniProt
Entry: A0A2S4YKF0_9ACTN
LinkDB: A0A2S4YKF0_9ACTN
Original site: A0A2S4YKF0_9ACTN 
ID   A0A2S4YKF0_9ACTN        Unreviewed;       478 AA.
AC   A0A2S4YKF0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:POX49417.1};
GN   ORFNames=C3489_24815 {ECO:0000313|EMBL:POX49417.1};
OS   Streptomyces sp. Ru71.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX49417.1, ECO:0000313|Proteomes:UP000237414};
RN   [1] {ECO:0000313|EMBL:POX49417.1, ECO:0000313|Proteomes:UP000237414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru71 {ECO:0000313|EMBL:POX49417.1,
RC   ECO:0000313|Proteomes:UP000237414};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-2018) 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}.
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:POX49417.1}.
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DR   EMBL; PQSS01000047; POX49417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4YKF0; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000237414; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000237414}.
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   478 AA;  49414 MW;  5EC53403AF868468 CRC64;
     MATAPSVSYS MTIRLEVPAS GTAVSQLTTA VESSGGSVTG LDVTASGHEK LRIDVTIAAT
     STAHAEEIVG KLRTIEGVTL GKVSDRTFLM HLGGKIEMAS KHPIRNRDDL SMVYTPGVAR
     VCMAIAENPE DARRLTIKRN SVAVVTDGSA VLGLGNIGPK AALPVMEGKA ALFKRFAGID
     AWPICLDTQD TDAIVEIVKA IAPGFAGINL EDISAPRCFE IEARLREALD IPVFHDDQHG
     TAIVVLASLT NALRVVGKGI GDVRVVMSGA GAAGTAILKL LLAAGVKNAV VADIQGVVHA
     GREDLVDAPA DSALRWIADN TNPENLTGTL KEAVRGADVF IGVSAPNVLD GDDVAAMAEG
     AIVFALANPD PEVDPAIARQ TAAVVATGRS DFPNQINNVL VFPGVFRGLL DAQSRTVNTE
     MMLAAAKALA DVVTEDELNP NYIIPSVFND KVAGAVAGAV RDAAKAAGAA AKTDDTAV
//
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