ID A0A371IMK2_9FIRM Unreviewed; 342 AA.
AC A0A371IMK2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN ORFNames=BBG48_003665 {ECO:0000313|EMBL:RDY21735.1}, FL857_00500
GN {ECO:0000313|EMBL:TRW28797.1};
OS Criibacterium bergeronii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Criibacterium.
OX NCBI_TaxID=1871336 {ECO:0000313|EMBL:RDY21735.1, ECO:0000313|Proteomes:UP000093352};
RN [1] {ECO:0000313|EMBL:RDY21735.1, ECO:0000313|Proteomes:UP000093352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY21735.1,
RC ECO:0000313|Proteomes:UP000093352};
RX PubMed=27587833;
RA Maheux A.F., Berube E., Boudreau D.K., Raymond F., Corbeil J., Roy P.H.,
RA Boissinot M., Omar R.F.;
RT "Draft Genome Sequence of Criibacterium bergeronii gen. nov., sp. nov.,
RT Strain CCRI-22567T, Isolated from a Vaginal Sample from a Woman with
RT Bacterial Vaginosis.";
RL Genome Announc. 4:e00959-16(2016).
RN [2] {ECO:0000313|EMBL:RDY21735.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY21735.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TRW28797.1, ECO:0000313|Proteomes:UP000319424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-24246 {ECO:0000313|EMBL:TRW28797.1,
RC ECO:0000313|Proteomes:UP000319424};
RA Maheux A.F., Boudreau D.K., Berube E., Brodeur S., Bernard K.A., Abed J.Y.,
RA Ducrey E., Guay E.F., Raymond F., Corbeil J., Domingo M.-C., Roy P.H.,
RA Boissinot M., Tocheva E.I., Omar R.F.;
RT "Criibacterium bergeronii gen. nov., sp. nov. isolated from human clinical
RT samples.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC heptulosonate-7-phosphate (DAHP). {ECO:0000256|ARBA:ARBA00003726,
CC ECO:0000256|PIRNR:PIRNR001361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00001370,
CC ECO:0000256|PIRNR:PIRNR001361};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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:RDY21735.1}.
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; MBEW02000005; RDY21735.1; -; Genomic_DNA.
DR EMBL; VJXW01000001; TRW28797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371IMK2; -.
DR STRING; 1871336.BBG48_00070; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000093352; Unassembled WGS sequence.
DR Proteomes; UP000319424; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DAHP_synth_1.
DR NCBIfam; TIGR00034; aroFGH; 1.
DR PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR PIRSF; PIRSF001361; DAHP_synthase; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Reference proteome {ECO:0000313|Proteomes:UP000093352};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 31..331
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 342 AA; 38923 MW; 59DC00165BA3EF59 CRC64;
MNFHQKLPIP KDIKQQYPVT EQMANVKKQR DIELKNIFEG KSNKFLLIVG PCSADNKKSV
MDYVERLRNL QEKVKDNIFI IPRVYTNKPR TTGEGYKGML HQPVPTQKPD MLEGIIASRD
LHMSILNEYG FSCADEMLYP DNLRYFSDVL SYVAVGARSV ENQQHRLTAS GLDVPVGMKN
PTSGELSVLM NSIKAAQIGH TFIYRGWEVD SSGNPYAHAI LRGYQDPTGR AIPNYHYEDI
LTLNELYQKS NLENPAIIVD VNHSNSGKRY LEQIRIARDV LYSRNQSKKI KTIVKGLMIE
SYLIDGCQKP DGNTYGQSIT DPCLGWEKTE KLIYEIADTL NK
//
