ID C8W3C7_DESAS Unreviewed; 350 AA.
AC C8W3C7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000313|EMBL:ACV61894.1};
DE EC=2.5.1.54 {ECO:0000313|EMBL:ACV61894.1};
GN OrderedLocusNames=Dtox_1008 {ECO:0000313|EMBL:ACV61894.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61894.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV61894.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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DR EMBL; CP001720; ACV61894.1; -; Genomic_DNA.
DR RefSeq; WP_015756609.1; NC_013216.1.
DR AlphaFoldDB; C8W3C7; -.
DR STRING; 485916.Dtox_1008; -.
DR KEGG; dae:Dtox_1008; -.
DR eggNOG; COG2876; Bacteria.
DR HOGENOM; CLU_062599_0_0_9; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000002217; 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; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006268; DAHP_syn_2.
DR NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR43018:SF1; PROTEIN AROA(G); 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW Transferase {ECO:0000313|EMBL:ACV61894.1}.
FT DOMAIN 87..320
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 350 AA; 38129 MW; D4814AB0D0D7ECB7 CRC64;
MLIEFNRFAP EKDIDLVLGR LNDEGVLAFR TRSNMNPVIV STLKVDGLKK LNIEGVASVQ
RVVEVSTPFK LASRAFKKTD TVVKVDNLEI GGDKIHVMAG PCAVESREQL LKTAHTVKAC
GATFLRGGAF KPRTSPYSFQ GLNEDGLKFL AEARTLTGLK IVTEVMDTRS VQLVAKYADV
LQIGARNMQN FDLLKEVGRV SKPVLLKRGA NATIEEFLAA AEYVLAGGNE DVILCERGVR
GVNEFTRYTL DIAAVPVLKK LTHLPVVVDP SHATGHWNYV EPMAMASLAA GADGLIIEVH
PEPEKALCDG AQSLTPKNFT VLMLRLAGLQ NSVCRDLAVP DMHLQQLDIS
//
