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 13-SEP-2023, entry version 74.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; 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 OrthoDB; 9771504at2; -.
DR BioCyc; MetaCyc:MONOMER-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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 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
//
