GenomeNet

Database: UniProt
Entry: A0A0B9ATX3_BRELN
LinkDB: A0A0B9ATX3_BRELN
Original site: A0A0B9ATX3_BRELN 
ID   A0A0B9ATX3_BRELN        Unreviewed;       401 AA.
AC   A0A0B9ATX3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)) {ECO:0000313|EMBL:KHS52783.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:KHS52783.1};
GN   ORFNames=AE0388_1766 {ECO:0000313|EMBL:KHS52783.1};
OS   Brevibacterium linens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS52783.1, ECO:0000313|Proteomes:UP000031488};
RN   [1] {ECO:0000313|EMBL:KHS52783.1, ECO:0000313|Proteomes:UP000031488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AE038-8 {ECO:0000313|EMBL:KHS52783.1,
RC   ECO:0000313|Proteomes:UP000031488};
RA   Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT   "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL   Submitted (NOV-2014) 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:KHS52783.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JTJZ01000018; KHS52783.1; -; Genomic_DNA.
DR   RefSeq; WP_052239930.1; NZ_JTJZ01000018.1.
DR   AlphaFoldDB; A0A0B9ATX3; -.
DR   STRING; 1703.BLSMQ_0593; -.
DR   PATRIC; fig|1703.6.peg.1649; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000031488; Unassembled WGS sequence.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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; 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   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   Oxidoreductase {ECO:0000313|EMBL:KHS52783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031488}.
FT   DOMAIN          30..163
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          175..395
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        51
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        106
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   401 AA;  41551 MW;  E181F560876CFED2 CRC64;
     MTTTAHNSAA SDQGSKGPIT DAEIFEAHEG GKLSAELTSP LQTQRDLSIA YTPGVAKVCT
     AIKDEPQLAR THTWTGRLVA VISDGSAVLG LGDIGPAASL PVMEGKCALF KSFSGLNAIP
     IVLDTNDTDE IVETIVRMAP TFGAINLEDI SAPRCFEIED RVKEALDIPV MHDDQHGTAV
     VVLAALTNAL RVVKKSFESV RVVVSGAGAA GVAVVKLLAD AGVKDIVVLD SKGVVESGRS
     DLSETKQFLA ESTNPRGISG GIGEALDGAD AFIGVSGGTI DEAHLENMAD DAIIFALSNP
     NPEVAPDVAS KYATVVATGR SDFPNQINNV LAFPGIFRGA LDADANEITD DMKLVAARAI
     ADLVGDDLEP GYIVPGALDS RVAPAVAEAV EKSALEAMAK R
//
DBGET integrated database retrieval system