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Database: UniProt
Entry: K9XG81_9CHRO
LinkDB: K9XG81_9CHRO
Original site: K9XG81_9CHRO 
ID   K9XG81_9CHRO            Unreviewed;       348 AA.
AC   K9XG81;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-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   ORFNames=Glo7428_2149 {ECO:0000313|EMBL:AFZ30672.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30672.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ30672.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30672.1,
RC   ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003646; AFZ30672.1; -; Genomic_DNA.
DR   RefSeq; WP_015188545.1; NC_019745.1.
DR   AlphaFoldDB; K9XG81; -.
DR   STRING; 1173026.Glo7428_2149; -.
DR   KEGG; glp:Glo7428_2149; -.
DR   PATRIC; fig|1173026.3.peg.2295; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_3; -.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000010476; 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:UP000010476};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:AFZ30672.1}.
FT   DOMAIN          45..337
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   348 AA;  38288 MW;  F714BB2891C212EC CRC64;
     MHNKLFNTHI QDSHILMTPK EVKAKLPLTH SAEKTVLRAR KEIEAILEGY DNRKFIVVGP
     CSIHDVKAAK EYAEKLKKLA DQVKDKLLLI MRVYFEKPRT NVGWKGLIND PDMNDSFHIE
     KGLLIARKLL IHLAELGLPA ATEALDPIVP QYISELIAWS AIGARTTESQ THREMASGLS
     MPVGFKNGTD GGIEVALNAL KSAEVPHHFL GINHNGQVSV FKTKGNTHGH IILRGGGGKP
     NYDPESIKAA EEKLKAANLP AKIVIDCSHG NSNKDYKLQA TVFNNVVQQI VEGNTAIVGM
     MLESNLYEGG QSIPSNLADL KYGVSVTDKC ISWEETEGII SDAYEKLK
//
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