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Database: UniProt
Entry: A0A0J5GXJ3_9BACI
LinkDB: A0A0J5GXJ3_9BACI
Original site: A0A0J5GXJ3_9BACI 
ID   A0A0J5GXJ3_9BACI        Unreviewed;       396 AA.
AC   A0A0J5GXJ3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KMJ58748.1};
GN   ORFNames=AB685_06595 {ECO:0000313|EMBL:KMJ58748.1};
OS   Bacillus sp. LL01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1665556 {ECO:0000313|EMBL:KMJ58748.1, ECO:0000313|Proteomes:UP000036436};
RN   [1] {ECO:0000313|EMBL:KMJ58748.1, ECO:0000313|Proteomes:UP000036436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL01 {ECO:0000313|EMBL:KMJ58748.1,
RC   ECO:0000313|Proteomes:UP000036436};
RA   Vilo C., Galetovic A., Araya J., Gomez Silva B., Dong Q.;
RT   "Draft Genome Sequence of a Bacillus Bacterium from the Atacama Desert
RT   Wetlands Metagenome.";
RL   Submitted (JUN-2015) 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KMJ58748.1}.
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DR   EMBL; LFEL01000002; KMJ58748.1; -; Genomic_DNA.
DR   RefSeq; WP_047969805.1; NZ_LFEL01000002.1.
DR   AlphaFoldDB; A0A0J5GXJ3; -.
DR   PATRIC; fig|1665556.3.peg.2275; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000036436; Unassembled WGS sequence.
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; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
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.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..386
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        39
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   396 AA;  41920 MW;  3D56F3F55FDD7D28 CRC64;
     MKGTNLKEKA LNLHREHAGK IAVVSKIDIH TEDDLSLAYT PGVGDVCKEI AKDPSKINSL
     TSRGNMVAVV TDGTAVLGLG DIGPKAAMPV MEGKSILFKQ FADIDAFPIC LDTKDVDEIV
     SIVKALQPTF AGINLEDIAA PRCFEIEERL KKELDIPVFH DDQHGTAIVV LGGLINALKL
     VKKPMETTKI VINGAGAAGI SIAKLLLTAG FADITLVSLE GIVCEGLDWL NDSQADISKR
     TNLHQINGTL NEAISGADVF IGVSGPAALN QSHIMKMAKD PVVFALANPI PEIYPEEALA
     AGAAVVGTGR SDYPNQINNL LAFPGIFRGA IDSGATNITE EMKIAAAYAI AKMIPEKELR
     ADNIIPRALD KQVAVEVSMA VANIANKKSD RSSSVS
//
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