AROG_HAEIN
ID AROG_HAEIN Reviewed; 362 AA.
AC P44303;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase;
DE EC=2.5.1.54;
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE AltName: Full=DAHP synthase;
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN Name=aroG; OrderedLocusNames=HI_1547;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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).
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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; L42023; AAC23197.1; -; Genomic_DNA.
DR PIR; I64128; I64128.
DR RefSeq; NP_439696.1; NC_000907.1.
DR AlphaFoldDB; P44303; -.
DR SMR; P44303; -.
DR STRING; 71421.HI_1547; -.
DR EnsemblBacteria; AAC23197; AAC23197; HI_1547.
DR KEGG; hin:HI_1547; -.
DR PATRIC; fig|71421.8.peg.1618; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR OMA; DINTGLR; -.
DR PhylomeDB; P44303; -.
DR BioCyc; HINF71421:G1GJ1-1567-MON; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DHAP_synth_1.
DR PANTHER; PTHR21225; PTHR21225; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR PIRSF; PIRSF001361; DAHP_synthase; 1.
DR TIGRFAMs; TIGR00034; aroFGH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..362
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase"
FT /id="PRO_0000140830"
SQ SEQUENCE 362 AA; 39937 MW; 533B76F7B379CD2D CRC64;
MAKEKIEIVV ANDDTRIEKV DQVLPPIALL EKYPASEQAA ALVKQTRHEA HNIIHGKDDR
LLVVIGPCSI HDPKAAIEYA TRLKPLREKY KDSLEIIMRV YFEKPRTTVG WKGLINEPYL
NDTYRLNDGL RIARKLLSDI NDLGVPAAGE FLDMITPQYL ADFMSWGAIG ARTTESQVHR
ELASGLSCAV GFKNATNGGV KVALDAIGAA EAPHYFLSVT KFGHSAIVST KGNEDCHIIL
RGGDKGPNYS AEDVEKVCAD IEKTGRIPHV MVDFSHANSS KQYKKQMDVC QDVCNQIAFG
SKQIFGVMVE SHLVEGRQDL VDGKAQTYGQ SITDACIGWE DSERLLQQLS DAVIARRKAT
SN