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Database: UniProt
Entry: D0IAJ6_GRIHO
LinkDB: D0IAJ6_GRIHO
Original site: D0IAJ6_GRIHO 
ID   D0IAJ6_GRIHO            Unreviewed;       355 AA.
AC   D0IAJ6;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=VHA_002773 {ECO:0000313|EMBL:EEY70914.1};
OS   Grimontia hollisae CIP 101886.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY70914.1, ECO:0000313|Proteomes:UP000003604};
RN   [1] {ECO:0000313|EMBL:EEY70914.1, ECO:0000313|Proteomes:UP000003604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY70914.1,
RC   ECO:0000313|Proteomes:UP000003604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA   Bartels D., Vonstein V.;
RL   Submitted (OCT-2009) 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:EEY70914.1}.
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DR   EMBL; ADAQ01000013; EEY70914.1; -; Genomic_DNA.
DR   RefSeq; WP_005505466.1; NZ_ADAQ01000013.1.
DR   AlphaFoldDB; D0IAJ6; -.
DR   GeneID; 58897669; -.
DR   eggNOG; COG0722; Bacteria.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000003604; 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:SF6; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TRP-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|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003604};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:EEY70914.1}.
FT   DOMAIN          44..339
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  38857 MW;  3D5F64C834C78FA5 CRC64;
     MPIKTDELRT QPIDTLPTPA EVEADSPLTD SVAQHIADAR KRVEDILTGR DNRLLVVVGP
     CSIHDPVAGL DYATRLKALA DKHKDNLLIV MRTYFEKPRT VVGWKGMIND PDLDGSCNLR
     EGLFKARKFL VDVNTLGMPT ATEFLDMVTG QYIADLVTWG AIGARTTESQ IHREMASALS
     CPVGFKNGTD GNIKIAIDAI RSSQTSHLFC SPDKHGVMTI YRTSGNPYGH VILRGGHQPN
     YSKADVAAAA ANLSAFNLTP RLLVDFSHAN CQKQHKRQLD IAADVCNQLV EGDVFIAGIM
     AESFIEEGNQ PVDKENIHAL TYGKSITDPC LGWDDTAVML QMLSDAVAKR NRTFA
//
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