(data stored in ACNUC7421 zone)

SWISSPROT: Q47SG7_THEFY

ID   Q47SG7_THEFY            Unreviewed;       428 AA.
AC   Q47SG7;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 108.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate decarboxylating) {ECO:0000313|EMBL:AAZ54600.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:AAZ54600.1};
GN   OrderedLocusNames=Tfu_0562 {ECO:0000313|EMBL:AAZ54600.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54600.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54600.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0562; -.
DR   EnsemblBacteria; AAZ54600; AAZ54600; Tfu_0562.
DR   KEGG; tfu:Tfu_0562; -.
DR   eggNOG; ENOG4105C6K; Bacteria.
DR   eggNOG; COG0281; LUCA.
DR   HOGENOM; HOG000132447; -.
DR   KO; K00027; -.
DR   OMA; ILFKQFG; -.
DR   BioCyc; TFUS269800:G1G4Q-573-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
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; 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; 2.
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;
DR   PRODOM; Q47SG7.
DR   SWISS-2DPAGE; Q47SG7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Oxidoreductase {ECO:0000313|EMBL:AAZ54600.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       56    189       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      201    421       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE     77     77       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    132    132       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       174    174       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       175    175       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       200    200       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   428 AA;  45069 MW;  E55DCAE05E53EFB2 CRC64;
     MSHKPHLRPS PLAASHRTLS PSTWMGTRTD SLRGFYVTSD RSSRLDDDPA FALHRGGKLE
     VRSTVEVNDQ KSLSLAYTPG VARVCTAIAD TPELADTYTW KNNVVAVVTD GTAVLGLGDI
     GPEASLPVME GKSLLFKQFA GIDSVPIALA CTDVDEIVET VVRMAPSFGG INLEDISAPR
     CFEIEQRLRE RLDIPVFHDD QHGTAIVALA AIRNAARVTG RELSDLRAVV SGAGASGIAV
     SRMLIRGGIG DIAVADSKGL IYEGRPGLNK YKAELAAISN KAGLQGSIES ALAGADVFVG
     LSAGEVPEEV VATMADNAII CAMANPNPEV HPDVARKYAA VVATGRSDFP NQINNVLAFP
     GVFRGALDVR ATQITENMKL AAATALADLV GDDLAPDYII PKPFDERVVP AVAAAVADQA
     RKDGVARA
//

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