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Database: UniProt
Entry: A0A0X1RV14_9BACL
LinkDB: A0A0X1RV14_9BACL
Original site: A0A0X1RV14_9BACL 
ID   A0A0X1RV14_9BACL        Unreviewed;       394 AA.
AC   A0A0X1RV14;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 9.
DE   SubName: Full=Malic enzyme, NAD binding domain protein {ECO:0000313|EMBL:AMA62350.1};
GN   ORFNames=ASO14_387 {ECO:0000313|EMBL:AMA62350.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA62350.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA62350.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA62350.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|RuleBase:RU003427}.
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DR   EMBL; CP013217; AMA62350.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMA62350; AMA62350; ASO14_387.
DR   KEGG; kur:ASO14_387; -.
DR   PATRIC; fig|1750719.3.peg.363; -.
DR   KO; K00027; -.
DR   Proteomes; UP000058129; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   Gene3D; 3.40.50.10380; -; 1.
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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000058129};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058129}.
FT   DOMAIN       13    146       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      158    382       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE     34     34       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       131    131       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       132    132       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   394 AA;  42334 MW;  26E3313117F462F5 CRC64;
     MSRESLELHE NLRGKMKLQP KIEVKSSKEL SLVYSPGVAE PCLAIQQNPK KVYDYTMKGN
     LVGVVSDGTA VLGLGDIGPK AAMPVMEGKA LLLQQLAGVD AMPICLDTKD VDEIVMIVKN
     IAPTFGAINL EDISAPRCFE IEDRLRKECG IPVFHDDQHG TAIVVSAGLR NALKVVGKQK
     ENVKVVINGA GAAGVAVMKL LLTMGYQHVT ACDSKGIIYK GRPYGMNAEK EYMANLSSAE
     HQEGTLADAL VGADIFIGVS VANVLTESMI QSMNQDPIVF ALANPNPEIT YEHAMEWGVR
     VIATGRSDYP NQVNNMLAFP GIFKGALAVQ ATDINDEMKM AAVKAISELV TAEQIERGIV
     IPNVFETDVT DDVAQAVMQA AIDSKVAQKI PSLI
//
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