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Database: UniProt
Entry: A0A0C9ND67_SPHPI
LinkDB: A0A0C9ND67_SPHPI
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ID   A0A0C9ND67_SPHPI        Unreviewed;       457 AA.
AC   A0A0C9ND67;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE            EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN   Name=aroF {ECO:0000313|EMBL:GAN14242.1};
GN   ORFNames=SP6_33_00450 {ECO:0000313|EMBL:GAN14242.1};
OS   Sphingomonas paucimobilis NBRC 13935.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14242.1, ECO:0000313|Proteomes:UP000032025};
RN   [1] {ECO:0000313|EMBL:GAN14242.1, ECO:0000313|Proteomes:UP000032025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14242.1,
RC   ECO:0000313|Proteomes:UP000032025};
RA   Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA   Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL   Submitted (AUG-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   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAN14242.1}.
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DR   EMBL; BBJS01000033; GAN14242.1; -; Genomic_DNA.
DR   RefSeq; WP_007404646.1; NZ_BBJS01000033.1.
DR   AlphaFoldDB; A0A0C9ND67; -.
DR   GeneID; 78528592; -.
DR   Proteomes; UP000032025; Unassembled WGS sequence.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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   Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
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         291
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         322
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         396
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         426
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ   SEQUENCE   457 AA;  50230 MW;  29DE36D1B487CC17 CRC64;
     MAANWAPNSW TSAEARQLPE YPDAQALDAA TRTLSSYPPL VFAGEARNLT AELAEVAAGR
     GFLLQGGDCA ESFAEHSANN IRDTFRVILQ MAVVLTFASK LPVVKLGRMA GQFAKPRSAN
     TEVVDGVELP SYRGDNVNDI AFTPEARIPD PQRMLRSYAQ SAATLNLLRA FAQGGYANLH
     QVHRWTHDFM GRSPWARKYS EMADRIGEAL DFMAACGIDP ASVPQLAQTS FYTSHEALLL
     PYEQALTRQD SLTGDWYDTS AHFLWIGDRT RFEGSAHVEF LRGIGNPIGV KCGPSLEPEA
     LLRMLDTLNP GRVPGRITLI TRYGHDKIEA HLPKLVRAVT REGHPVVWSC DPMHGNTIKA
     ATGYKTRPFD RILAEVRGFF AVHRAEGTHA GGIHAEMTGQ NVTECTGGAI DVTEQSLADR
     YHTHCDPRLN AGQSLEMAFL LAEMLNEEMA ERRKAAA
//
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