ID   GRIH_STRGR              Reviewed;         396 AA.
AC   A0JC76;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=3-amino-4-hydroxybenzoic acid synthase;
DE            Short=3,4-AHBA synthase;
DE            EC=4.1.99.20 {ECO:0000269|PubMed:17003031};
GN   Name=griH;
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, SUBUNIT, ACTIVITY REGULATION, AND COFACTOR.
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 the cyclization of 2-amino-4,5-dihydroxy-6-one-
CC       heptanoic acid-7-phosphate to yield 3-amino-4-hydroxybenzoic acid (3,4-
CC       AHBA). {ECO:0000269|PubMed:17003031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = 3-
CC         amino-4-hydroxybenzoate + H(+) + 2 H2O + phosphate;
CC         Xref=Rhea:RHEA:26317, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58898, ChEBI:CHEBI:60005;
CC         EC=4.1.99.20; Evidence={ECO:0000269|PubMed:17003031};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:17003031};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:17003031};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:17003031};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17003031};
CC       Note=Manganese. Cobalt, iron and magnesium can be used to a lesser
CC       extent. {ECO:0000269|PubMed:17003031};
CC   -!- ACTIVITY REGULATION: Partially inhibited by 0.1 mM pyridoxal phosphate.
CC       {ECO:0000269|PubMed:17003031}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12 uM for 2-amino-4,5-dihydroxy-6-one-heptanoic acid-7-phosphate
CC         (at 30 degrees Celsius) {ECO:0000269|PubMed:17003031};
CC         Note=This Km value might be underestimated because the concentration
CC         of the substrate determined is perhaps lower than the actual
CC         concentration due to the instability of the substrate compound.;
CC       pH dependence:
CC         Optimum pH is 6.5-10.5. {ECO:0000269|PubMed:17003031};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:17003031};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17003031}.
CC   -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family. GriH
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB259663; BAF36650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0JC76; -.
DR   OMA; HFGMAIK; -.
DR   BioCyc; MetaCyc:MON-17798; -.
DR   BRENDA; 4.1.99.20; 6035.
DR   SABIO-RK; A0JC76; -.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase 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   InterPro; IPR002812; DHQ_synth.
DR   PANTHER; PTHR33563; PTHR33563; 1.
DR   Pfam; PF01959; DHQS; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Manganese.
FT   CHAIN           1..396
FT                   /note="3-amino-4-hydroxybenzoic acid synthase"
FT                   /id="PRO_0000361907"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  42438 MW;  C61B33EDA34C1201 CRC64;
     MSSSPSPSPS SSSSSSASSS ASSSPSSSSK LTWLDIRSVG EARAAIVQEA LHHRVEALVA
     DDPAHLADLP PTVAKVLLVV GKQIPEEFGE ATVVVVDPSK HGVTPAELAL KHPEIEFGRF
     VEIIDAPTLE DACESSRTEK WSVLLFRDPT KIPLEIVIAA AARASGSMVT IAQDLEEAEI
     LFGVLEHGSD GVMMAPKTVG DAAELKRIAE AGIPNLNLTE LRVVETSHIG MGERACVDTT
     THFGEDEGIL VGSHSKGMIL CVSETHPLPY MPTRPFRVNA GAIHSYTLGR DERTNYLSEL
     KTGSKLTAVD IKGNTRLVTV GRVKIETRPL ISIDAEAPDG RRVNLILQDD WHVRVLGPGG
     TVLNSTELKP GDTVLGYLPV EDRHVGYPIN EFCLEK