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Database: UniProt
Entry: D4H213_DENA2
LinkDB: D4H213_DENA2
Original site: D4H213_DENA2 
ID   D4H213_DENA2            Unreviewed;       351 AA.
AC   D4H213;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=Dacet_0185 {ECO:0000313|EMBL:ADD66990.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD66990.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD66990.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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}.
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DR   EMBL; CP001968; ADD66990.1; -; Genomic_DNA.
DR   RefSeq; WP_013009538.1; NC_013943.1.
DR   AlphaFoldDB; D4H213; -.
DR   STRING; 522772.Dacet_0185; -.
DR   PaxDb; 522772-Dacet_0185; -.
DR   KEGG; dap:Dacet_0185; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_0; -.
DR   InParanoid; D4H213; -.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000002012; 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:SF10; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYR-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:UP000002012};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:ADD66990.1}.
FT   DOMAIN          48..344
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   351 AA;  38842 MW;  AB9E7D886E69092B CRC64;
     MSPSQRIETN NINVFEVTPI IEPQYLKQVF PMPLDGDAFV DKSRNAIKDI LNGKDKRLLA
     VVGPCSIHDT NAALEYAGRL RELSEKVQDK ILIIMRVYFE KPRTTVGWKG LINDPDLNGT
     YQISKGLGMA RQLYCSITEL GLPIAAEMLD PITPQYLSDM ISWGAIGART TESQTHREMA
     SGLSFPVGFK NGTDGGLKIA IDAMSAACRE HSFLGINYEG VTAIVHTKGN PDVHIVLRGG
     NDSPNYYKKD IEETVTLLSD NHLPPAIMVD CSHANSYKDH KRQGEVLDSV VEQIRAGQTA
     IKGVMIESNI YCGNQSIPDD LSQLKYGVSV TDKCVDWETT EEMLTDAHRR L
//
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