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Database: UniProt
Entry: D4H702_DENA2
LinkDB: D4H702_DENA2
Original site: D4H702_DENA2 
ID   D4H702_DENA2            Unreviewed;       339 AA.
AC   D4H702;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   13-NOV-2019, entry version 43.
DE   SubName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000313|EMBL:ADD69706.1};
DE            EC=2.5.1.54 {ECO:0000313|EMBL:ADD69706.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Dacet_2956 {ECO:0000313|EMBL:ADD69706.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / N2460).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD69706.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD69706.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / N2460 {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Detter J.C., Brettin T., Spring S.,
RA   Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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DR   EMBL; CP001968; ADD69706.1; -; Genomic_DNA.
DR   RefSeq; WP_013012191.1; NC_013943.1.
DR   STRING; 522772.Dacet_2956; -.
DR   EnsemblBacteria; ADD69706; ADD69706; Dacet_2956.
DR   KEGG; dap:Dacet_2956; -.
DR   eggNOG; ENOG4108JPM; Bacteria.
DR   eggNOG; COG2876; LUCA.
DR   HOGENOM; HOG000023020; -.
DR   KO; K03856; -.
DR   OMA; VIVMKPN; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; DACE522772:G1GHO-2981-MONOMER; -.
DR   Proteomes; UP000002012; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR041071; DAHP_snth_FXD.
DR   InterPro; IPR006268; DAHP_syn_2.
DR   Pfam; PF18152; DAHP_snth_FXD; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   TIGRFAMs; TIGR01361; DAHP_synth_Bsub; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:ADD69706.1}.
FT   DOMAIN        1     67       DAHP_snth_FXD. {ECO:0000259|Pfam:
FT                                PF18152}.
FT   DOMAIN       83    319       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   339 AA;  36956 MW;  796DDC98AE11F23D CRC64;
     MIIVFKKGTE KENIANVQKK LESYGFKVHL SEGVETTIMG AIGDESTLRD KPLSSFPGVE
     KVVPIVKPYK LVSKDFRKED TVIDVKGIKL GGGNVVVMAG PCSVEGRDML FEIAGRASKA
     GAKILRGGAF KPRTSPYAFQ GLGEEGLKYL REAADAHGML VITELMDPRD IDLICKYTDI
     IQIGARNMQN FRLLRDLGEL RKPVMLKRGL CATMKELLMA AEYVAAGGNN EIILCERGIR
     TFETETRNTL DLSAIPVLKS LTHLPVVADP SHGTGRRDCI LPMSQAAVAA GADGIIVEVH
     NCPEEAMSDG DQSILPDDFD ILMKRIDIIA QTIGKTLNK
//
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