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Entry: A0A075JEB7_9MICO
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ID   A0A075JEB7_9MICO        Unreviewed;       446 AA.
AC   A0A075JEB7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE            EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN   ORFNames=HX89_06190 {ECO:0000313|EMBL:AIF40596.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40596.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF40596.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF40596.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363071};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC       manganese, cobalt or cadmium ions. {ECO:0000256|PIRSR:PIRSR602480-1};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|RuleBase:RU363071}.
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
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DR   EMBL; CP008889; AIF40596.1; -; Genomic_DNA.
DR   RefSeq; WP_006946641.1; NZ_UFXX01000001.1.
DR   AlphaFoldDB; A0A075JEB7; -.
DR   GeneID; 41840762; -.
DR   KEGG; dni:HX89_06190; -.
DR   eggNOG; COG3200; Bacteria.
DR   HOGENOM; CLU_026885_0_1_11; -.
DR   OrthoDB; 9766852at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000027986; 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; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002480; DAHP_synth_2.
DR   NCBIfam; TIGR01358; DAHP_synth_II; 1.
DR   PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR   Pfam; PF01474; DAHP_synth_2; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW   Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027986};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         108
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         264..265
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         287
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         318
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         392
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         422
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ   SEQUENCE   446 AA;  49181 MW;  B81CBEDFC2445CA0 CRC64;
     MPTRPVGLEW PQLPAKQQPS WPDDGSLERV RETLATYPPL VFAGECDDLR TRLAAASRGE
     AFVLQGGDCA EMFASATADN IRDRVKTILQ MAAVLTYGAS TPVVKLGRIA GQFAKPRSKD
     TETRGDVTLP AYRGDMVNDF AFTPEARRPD PERLLQAYNT SAATLNLVRA FTQGGFADLR
     NVHDWNKGFI ANAANARYEK TAKDIDRAMR FMAACGVDFD ALRAVDFFSS HEALLLDYER
     PLTRVDSRSG RPYATSGHML WVGERTREID GAHIDFVSRV SNPVGMKVGP KADPDDLLRI
     IDKIDPEREP GRLTFITRMG AGTIREALPP IVERLKAEGA APVWITDPMH GNTFESASGF
     KTRRLDDIVD EVRGFFEVHE AAGTVPGGLH VELTGNDVTE CLGGSVEVRD EDLESRYESA
     CDPRLNHQQS LELAYLVAEM LSARAQ
//
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