ID A0A0Q9S1Q9_9BACL Unreviewed; 347 AA.
AC A0A0Q9S1Q9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000313|EMBL:KRF21474.1};
DE EC=2.5.1.54 {ECO:0000313|EMBL:KRF21474.1};
GN ORFNames=ASG93_08865 {ECO:0000313|EMBL:KRF21474.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF21474.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF21474.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF21474.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF21474.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF21474.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRF21474.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMSP01000023; KRF21474.1; -; Genomic_DNA.
DR RefSeq; WP_047677334.1; NZ_LMSP01000023.1.
DR AlphaFoldDB; A0A0Q9S1Q9; -.
DR STRING; 1736411.ASG93_08865; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
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; IPR041071; DAHP_snth_FXD.
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:SF2; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR Pfam; PF18152; DAHP_snth_FXD; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Transferase {ECO:0000313|EMBL:KRF21474.1}.
FT DOMAIN 1..67
FT /note="DAHP synthase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18152"
FT DOMAIN 82..324
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 347 AA; 37656 MW; 022FFD3EF49B62C6 CRC64;
MIAITSNKTS DERIQEIVQF VEKQGVQAHV SKGEDRTVIG IIGQADPKLA EQLRQMSGVE
QVVKISKSYK LASRDFHPAD TVIKIKGVEI GGEQLVVMGG PCAVETPEQI DEIARLVKAA
GGQVLRGGAF KPRTGPYSFQ GVGVEGLIMM AEAGKKHGLL TITEVMTPEY VDVCAQYADI
LQVGTRNMQN FDLLRKLGTI QTPVLLKRGF SSTYDEFLNA AEYILAGGNP NVMLCERGIR
TFETYTRNTL DLSAIPVLKQ LSHLPVISDP SHGTGRRELV VPMTKASVAA GADGLIIEMH
TDPDNSMTGD GVQSLFPDQF ANLLVDLEKL APLLGKKFDT HKEVILA
//
