ID   GRII_STRGR              Reviewed;         274 AA.
AC   A0JC77;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate synthase;
DE            EC=4.1.2.56;
GN   Name=griI;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=IFO 13350;
RX   PubMed=17003031; DOI=10.1074/jbc.m608103200;
RA   Suzuki H., Ohnishi Y., Furusho Y., Sakuda S., Horinouchi S.;
RT   "Novel benzene ring biosynthesis from C(3) and C(4) primary metabolites by
RT   two enzymes.";
RL   J. Biol. Chem. 281:36944-36951(2006).
CC   -!- FUNCTION: Catalyzes aldol condensation between L-aspartate-4-
CC       semialdehyde (ASA) and dihydroxyacetone phosphate (DHAP), to form 2-
CC       amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate.
CC       {ECO:0000269|PubMed:17003031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate =
CC         dihydroxyacetone phosphate + L-aspartate 4-semialdehyde;
CC         Xref=Rhea:RHEA:26313, ChEBI:CHEBI:57642, ChEBI:CHEBI:58898,
CC         ChEBI:CHEBI:537519; EC=4.1.2.56;
CC         Evidence={ECO:0000269|PubMed:17003031};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.6 uM for L-aspartate-4-semialdehyde (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:17003031};
CC         KM=140 uM for dihydroxyacetone phosphate (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:17003031};
CC       pH dependence:
CC         Optimum pH is 6.5-10.0. {ECO:0000269|PubMed:17003031};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:17003031};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:17003031}.
CC   -!- MISCELLANEOUS: 2-amino-4,5-dihydroxy-6-one-heptanoic acid-7-phosphate
CC       can be converted to 5-acetyl-1H-pyrrole-2-carboxylic acid (5,2-APC) by
CC       a non-enzymatic reaction.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. GriI subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB259663; BAF36651.1; -; Genomic_DNA.
DR   RefSeq; WP_012380462.1; NZ_UAVD01000056.1.
DR   AlphaFoldDB; A0JC77; -.
DR   SMR; A0JC77; -.
DR   GeneID; 6213293; -.
DR   PATRIC; fig|455632.4.peg.4329; -.
DR   OMA; CEYWGMP; -.
DR   BioCyc; MetaCyc:MON-17797; -.
DR   BRENDA; 4.1.2.56; 6035.
DR   SABIO-RK; A0JC77; -.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase.
FT   CHAIN           1..274
FT                   /note="2-amino-4,5-dihydroxy-6-oxo-7-
FT                   (phosphonooxy)heptanoate synthase"
FT                   /id="PRO_0000361267"
SQ   SEQUENCE   274 AA;  28851 MW;  88D038603BE5DBDF CRC64;
     MAPNAPFARS LRLQRLHHHD PDRLFIVPLD HSITDGPLSR AHRLDPLVGE LASHHVDGIV
     LHKGSLRHVD PEWFTRTSLI VHLSASTVHA PDPNAKYLVS SVEESLRMGA DAVSVHVNLG
     SEGERHQIAD MAAVAEACDR WNVPLLAMMY PRGPKIDDPR DPALVAHAVQ VAVDLGADLV
     KTLYVGSVAA MAEITAASPV PVVVVGGPRD SDESRILAYV DDALRGGAAG VAMGRNVFQA
     PDPGAMADKL SDLIHNSGTR GAARAPAGAA AGAA