ID H9UKQ7_SPIAZ Unreviewed; 355 AA.
AC H9UKQ7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN OrderedLocusNames=Spiaf_2052 {ECO:0000313|EMBL:AFG38100.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38100.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
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 ---------------------------------------------------------------------------
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; CP003282; AFG38100.1; -; Genomic_DNA.
DR RefSeq; WP_014456083.1; NC_017098.1.
DR AlphaFoldDB; H9UKQ7; -.
DR STRING; 889378.Spiaf_2052; -.
DR KEGG; sfc:Spiaf_2052; -.
DR PATRIC; fig|889378.3.peg.2039; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_12; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000007383; Chromosome.
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:UP000007383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 45..331
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 355 AA; 38422 MW; 2DF2A1D4CF853F9A CRC64;
MRFNTDDTRI QQLKPLIPPA ILMEDYPLSE AGSETVQNGR AAIESIVQGQ DDRLLVVIGP
CSIHDTAAAL EYAARLAEAR TQFADTLEIV MRVYFEKPRS RTGWKGLIND PLLDGSFQIN
RGLRVARELL VEISDMGLPI GCEFLDTISP QFIADTVSWG AIGARTTESQ IHRELASGLS
MPVGFKNGTD GNIDIAIDAI HAASIPHHFL SVTKQSVAAI VETKGNPGCH IILRGGKGGP
NYHEESVEAA AAKLHLAKLP AGMMIDCSHG NSSKKPERQP IVARDIADQL TRGSRHIFGV
MIESHLQGGS QKLTDPSQLQ YGVSITDACL SFADSLPVLE TLSEAVTSRR KVRGQ
//