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Database: UniProt
Entry: A0A073K2I6_9BACI
LinkDB: A0A073K2I6_9BACI
Original site: A0A073K2I6_9BACI 
ID   A0A073K2I6_9BACI        Unreviewed;       570 AA.
AC   A0A073K2I6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KEK20715.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:KEK20715.1};
GN   ORFNames=BAMA_15020 {ECO:0000313|EMBL:KEK20715.1};
OS   Bacillus manliponensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK20715.1, ECO:0000313|Proteomes:UP000027822};
RN   [1] {ECO:0000313|EMBL:KEK20715.1, ECO:0000313|Proteomes:UP000027822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK20715.1,
RC   ECO:0000313|Proteomes:UP000027822};
RA   Lai Q., Liu Y., Shao Z.;
RT   "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT   1A00708).";
RL   Submitted (JUN-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|RuleBase:RU003427}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KEK20715.1}.
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DR   EMBL; JOTN01000003; KEK20715.1; -; Genomic_DNA.
DR   RefSeq; WP_034637043.1; NZ_JOTN01000003.1.
DR   EnsemblBacteria; KEK20715; KEK20715; BAMA_15020.
DR   Proteomes; UP000027822; 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   Gene3D; 3.40.50.10380; -; 1.
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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; SSF51735; SSF51735; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000027822};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Oxidoreductase {ECO:0000313|EMBL:KEK20715.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027822}.
FT   DOMAIN       82    264       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      274    532       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE    105    105       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    178    178       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       249    249       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       250    250       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       273    273       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   570 AA;  62113 MW;  FE7369C853F0CE76 CRC64;
     MTKFTVSPNG DLETTLRGAE ILGTPLLNKG VAFTEEERKA LGLKGLLPPA VLTLDEQARR
     AYKQFCSQPD DLLKNVYLTA LHDRNEVLFY RLLTDHLREM LPIVYTPTVG TAIQRYSHEY
     RKPRGVYLSI DDPNGIEEAF ANIGATTDNT DLIVVTDGEG ILGIGDWGVG GINIAIGKLA
     VYTAAVGIDP SRVLPVILDV GTNREDLLTN PFYIGNRHPR VTGEMYDDFI DKFVKTVCNK
     FPNAMLHWED FSSQNARRIL DKYRDEVCTF NDDIQGTGAV SLAAVLSAVK ASGMPLCEHR
     VVVFGAGTAG IGIADQVRDA MVRDGLTEEE ANGRFWCIDR PGLLTDDMDN LLNFQVPYAR
     KVSEVEDWKQ NGTIGLADVV KHVKPTILIG TSTVAGAFSE EIVKEMASHV ERPIILPMSN
     PTPLAEAKPV DLMNWTEGRA LVATGSPFDP VTYDGVTYSI GQCNNALIFP GLGLGTIVVR
     ARLMTDAMFA AAAEAVVNMV DVSKQGAAIL PEVEELRTVS EAVAVAVAKA AVTEGVARNE
     MNDEEIEQAV KASMWQPVYR NVKAVEKVTV
//
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