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Database: UniProt
Entry: A0A139V2Z2_MYCPH
LinkDB: A0A139V2Z2_MYCPH
Original site: A0A139V2Z2_MYCPH 
ID   A0A139V2Z2_MYCPH        Unreviewed;       386 AA.
AC   A0A139V2Z2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   20-JUN-2018, entry version 12.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KXW60672.1};
GN   ORFNames=MPHL43239_24865 {ECO:0000313|EMBL:KXW60672.1};
OS   Mycobacterium phlei DSM 43239 = CCUG 21000.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1226750 {ECO:0000313|EMBL:KXW60672.1, ECO:0000313|Proteomes:UP000070233};
RN   [1] {ECO:0000313|EMBL:KXW60672.1, ECO:0000313|Proteomes:UP000070233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43239 \ CCUG 21000 {ECO:0000313|Proteomes:UP000070233};
RX   PubMed=26941228;
RA   Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S.,
RA   Bhattacharya A., Kirsebom L.A.;
RT   "The Mycobacterium phlei genome: expectations and surprises.";
RL   Genome Biol. Evol. 0:0-0(2016).
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   -!- 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:KXW60672.1}.
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DR   EMBL; ANBO01000044; KXW60672.1; -; Genomic_DNA.
DR   EnsemblBacteria; KXW60672; KXW60672; MPHL43239_24865.
DR   PATRIC; fig|1226750.3.peg.4963; -.
DR   Proteomes; UP000070233; Unassembled WGS sequence.
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; 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   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070233};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070233}.
FT   DOMAIN       20    153       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      165    385       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       138    138       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       139    139       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   386 AA;  39703 MW;  B3C83AAAEFBCD89B CRC64;
     MNTTSPLAVS DEEIFAAHLG GKLSSALKAP LDTERALSIA YTPGVAQVSR AIAADHTLAS
     RYTWANRLVA VVSDGSAVLG LGDIGAAASL PVMEGKSALF KAFADLDSIP IVLDTKDPDE
     IVETLVRLRP TFGAVNLEDI SAPRCFEIER RLIEALDCPV MHDDQHGTAI VVLAALLGAA
     KVVDREIPSL RVVVAGAGAA GVACAKILIA AGVSDITLLD SQGIIYKGRD KLNASKAEMA
     EVSNPRGLKG GLAEALAGAD VFLGLSGGVV PAELIDTMAP NSIVFALSNP DPEIHPGEAR
     HHAAVVATGR SDFPNQINNV LAFPGVFRGA LDAGARRITE QMKVAAAHAI HGVLGDDLSP
     EKIVPSALDT RVAPAVAQAV AAASGV
//
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