ID H6SRE3_PARPM Unreviewed; 899 AA.
AC H6SRE3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=RSPPHO_00846 {ECO:0000313|EMBL:CCG07472.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07472.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG07472.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; HE663493; CCG07472.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SRE3; -.
DR STRING; 1150469.RSPPHO_00846; -.
DR KEGG; rpm:RSPPHO_00846; -.
DR PATRIC; fig|1150469.3.peg.974; -.
DR eggNOG; COG3200; Bacteria.
DR HOGENOM; CLU_322067_0_0_5; -.
DR Proteomes; UP000033220; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000033220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT REGION 69..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 549
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 732
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 763
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 795
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 837
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 867
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 899 AA; 95953 MW; 341659CD8803ECA8 CRC64;
MSAACTTSSA PLSAGVTLGQ AIRARARGTG SARASAVHSD ARGLTRDSLA RQIAQQIVDG
HLGAGPFIHP LDDDGAGQTR PRGAIGQRLA GQGAGNDDGT GRHAAHEDLA GLAVDDPGRS
ADKHAHRQHG AGFDDHALGH FRTGANKAVV LNDHRPRLER LQHAADARAA RQMDIAPDLG
TGADGGPSVD HRALANASAQ IDEARHQDRP GSNIGRATHD ASGHGAKARL LKARSVPALE
LAGHLVPPDG AGRATGHDGH VGQAKGQQHR FLEPLMDGPG PVDLFRDAQG APIKAVQRRF
NGVAHRTVGG RGQSVALFPG GINDLAQGLV GHGVLVAPAN VLGRGPPAGP RVVGTREGVK
NRQREGLGRA TTIPPEAVKS TMAKGTKGGG ETKGRLGRRG LPRPLRSWAA FSLVRRKSLA
YIEPFSPKDL STPSHAKESP AMASTWTPDS WRLKPARQMP DYPDAAHLAA VEAELARFPP
LVFAGEARSL QSALARVGEG KAFLLQGGDC AESFAEFSAN TIRDTFRVML QMAVVLTFGA
ALPVVKVGRM AGQFAKPRSA PFETVEGKEL PSYRGDMVNA MDADLDARIP NPDRLLRVYH
QSAATLNLLR AFAQGGFAHL AQVHEWTLGF VQGSPQAERY GAFADRIAES LDFMHACGFT
AESVPQMRET DFYTSHEALL LNYEQALTRT DSLTGRWYGC SSHFLWVGDR TRELDGAHIE
YLRGIANPVG VKAGPSMKTD DLLRLCDVLN PHNEPGRLTI IVRMGAGKVT EGLPPLIRAI
TREGRNVVWS CDPMHANTVK ASSGYKTRDF LKILQEVTEF FAVHRAEGTH PGGVHFEMTG
ADVTECIGGA QEITEAALGD RYHTHCDPRL NASQSLELAF LIAEALKAER SRLRAQSRA
//
