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Database: UniProt
Entry: F2NL39_MARHT
LinkDB: F2NL39_MARHT
Original site: F2NL39_MARHT 
ID   F2NL39_MARHT            Unreviewed;       288 AA.
AC   F2NL39;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   22-NOV-2017, entry version 33.
DE   SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:AEB11442.1};
DE            EC=1.1.1.60 {ECO:0000313|EMBL:AEB11442.1};
GN   OrderedLocusNames=Marky_0692 {ECO:0000313|EMBL:AEB11442.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11442.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB11442.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M.,
RA   Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
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DR   EMBL; CP002630; AEB11442.1; -; Genomic_DNA.
DR   RefSeq; WP_013703494.1; NC_015387.1.
DR   STRING; 869210.Marky_0692; -.
DR   EnsemblBacteria; AEB11442; AEB11442; Marky_0692.
DR   KEGG; mhd:Marky_0692; -.
DR   eggNOG; ENOG4105CF3; Bacteria.
DR   eggNOG; COG2084; LUCA.
DR   OMA; QMFMQAS; -.
DR   OrthoDB; POG091H02BQ; -.
DR   Proteomes; UP000007030; Chromosome.
DR   GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029154; NADP-bd.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007030};
KW   Oxidoreductase {ECO:0000313|EMBL:AEB11442.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007030}.
FT   DOMAIN        2    158       NAD_binding_2. {ECO:0000259|Pfam:
FT                                PF03446}.
FT   DOMAIN      164    282       NAD_binding_11. {ECO:0000259|Pfam:
FT                                PF14833}.
FT   ACT_SITE    170    170       {ECO:0000256|PIRSR:PIRSR000103-1}.
SQ   SEQUENCE   288 AA;  30561 MW;  9B7B8676D75F1436 CRC64;
     MKVGILGTGI MGRPMARNLL EAGLEVWVWN RTREKAAPLL AAGARWAETP AALARQVDVL
     GLVLATPEAT REVFYREDGV LDGVHPGLFV VDHGTNPLAW AQEAAPLVAE AGGQYVDAPL
     QGSYPEAERR ALVILAGGTP TGLEPLSPYF EGVGGTIVFA GELGRGVLLK LALNLITALT
     GAALAEASAL AAAFGLGQEV FFEALEKSSL AAPFHRGKGE KLRSGDLSPQ LPLKLMNKDL
     RLIQAEASRV RFPLFMGGNA RALYTLAERM GLGEADLIAV RNVYREEA
//
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