ID V6KL97_STRNV Unreviewed; 891 AA.
AC V6KL97;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, 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=M877_03145 {ECO:0000313|EMBL:EST32788.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST32788.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST32788.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST32788.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:EST32788.1}.
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DR EMBL; AWQW01000026; EST32788.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KL97; -.
DR STRING; 193462.BBN63_00875; -.
DR PATRIC; fig|1352941.4.peg.643; -.
DR eggNOG; COG2124; Bacteria.
DR eggNOG; COG3200; Bacteria.
DR HOGENOM; CLU_324137_0_0_11; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000017971; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 CDD; cd11029; CYP107-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR002480; DAHP_synth_2.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 109
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 286
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 317
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 391
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 421
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 891 AA; 97395 MW; B5691AE8BA3414DD CRC64;
MTLTGEAAAH WRTLVAHQRP EWPSPAELGD VTGHLAASPP LVTPQECDTL TARLARAAEG
KAFLLQGGDC AERFDDLSAP AIHGKLRLLE QMAVVLSHAS AVPVATVGRI AGQYAKPRSR
PTETVDGRTL PVYRGDAVNG IGFSEAERRP DPARLLRMYD ASRHTLDVMR ARARAGTDRR
QLRKENQDFV SRSPAGERYG ELADRIGQAL SREDARGEGP SRTPEFFASH EGLLLDYEAA
LTRHHPRTGR RHAGSAHLLW IGDRTRQLDG AHVAYFATID NPIAVKLGPT ATPEQALALI
DRLDPDRRPG RLTFIVRMGA HRVRYLLPQL VEKVTASGAP VVWVCDPMHG NTFEAPSGHK
TRRFDDILAE VAGFFEVHKA LGTHVGGLHV ELTGEDVTEC LGGGAQLGLD DLHRRYESAC
DPRLNGDQAL ELAFLVAEMF DPGAAGVAAV NAERPGAHGT AVLPPRSARE PNNIFEEAPM
DQDSIPLELD DAFVQDPYAV YAKLAPEGSV HRVRMPPGVP VCGGLPVWLI IGYEAVRSAL
ADSRLSTDLN RMDGLFAQNE PDNNRRAGFS PAIASHMLNS DPPDHTRMRK LVSKAFTSRA
VEALRPEIER ITGELIDTLT DDDTVDLLDD FAFPLPIRVI CLLLGVPVEE QENFKSWSKA
LVSGDSPEAA AAATTEVVAY LGQLIERKRR EPTDDILTAL VAAHDDDHQL TETELVSTAY
LLFIAGFETT LNALGNGTLH LMRNLDQWEA LREDRSLLPG AVEEFLRLES PLKHASFRCA
TESLTIGDVE IPAGDFVLLA IASANRDPQR FDDPHALDVR RSTDGGHLAF GHGIHHCLGA
PLARVEVRVA FGALLDAFPA MRLAADPEEL RWRTSTIIRG LHSLPVRLNR R
//
