3HAPM_CUPPJ
ID 3HAPM_CUPPJ Reviewed; 471 AA.
AC Q46ZL2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=3-hydroxylaminophenol mutase;
DE Short=3HAP mutase;
DE EC=5.4.4.3;
DE AltName: Full=3-(hydroxyamino)phenol mutase;
GN OrderedLocusNames=Reut_A2057;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
RN [2]
RP PROTEIN SEQUENCE OF 2-42; 62-66 AND 120-134, FUNCTION AS A 3HAP MUTASE,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND REACTION MECHANISM.
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=10049374; DOI=10.1128/jb.181.5.1444-1450.1999;
RA Schenzle A., Lenke H., Spain J.C., Knackmuss H.J.;
RT "3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a
RT Bamberger rearrangement.";
RL J. Bacteriol. 181:1444-1450(1999).
RN [3]
RP PATHWAY.
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=16535572; DOI=10.1128/aem.63.4.1421-1427.1997;
RA Schenzle A., Lenke H., Fischer P., Williams P.A., Knackmuss H.;
RT "Catabolism of 3-nitrophenol by Ralstonia eutropha JMP 134.";
RL Appl. Environ. Microbiol. 63:1421-1427(1997).
CC -!- FUNCTION: Catalyzes the isomerization of 3-hydroxylaminophenol (3HAP)
CC to aminohydroquinone, a step in the degradative pathway of 3-
CC nitrophenol. The enzymatic reaction is regiospecific since it leads to
CC the formation of aminohydroquinone exclusively, without producing the
CC isomeric 4-aminocatechol. Can also isomerize other
CC hydroxylaminoaromatic compounds, such as hydroxylaminobenzene to a
CC mixture of 2-aminophenol and 4-aminophenol, 4-hydroxylaminotoluene to
CC 6-amino-m-cresol, and 2-chloro-5-hydroxylaminophenol to 2-amino-5-
CC chlorohydroquinone. Does not act on 4-hydroxylaminobenzoate.
CC {ECO:0000269|PubMed:10049374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyaminophenol = aminohydroquinone;
CC Xref=Rhea:RHEA:20577, ChEBI:CHEBI:13769, ChEBI:CHEBI:50446;
CC EC=5.4.4.3; Evidence={ECO:0000269|PubMed:10049374};
CC -!- ACTIVITY REGULATION: Is inhibited by H(2)O(2). 1,10-phenanthroline
CC inhibits the activity slightly, but other metal cation chelators such
CC as EDTA or tiron have no effect on the activity. Divalent metal cations
CC and hydroxylamine have also no effect on the activity. Due to the
CC relationship of the protein with glutamine synthetases, glutamate and
CC glutamine were tested as inhibitors; neither preincubation of the
CC compounds with the enzyme nor their addition to the assay buffer
CC affected 3HAP mutase activity. {ECO:0000269|PubMed:10049374}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for 3-hydroxyaminophenol {ECO:0000269|PubMed:10049374};
CC Vmax=4.8 umol/min/mg enzyme {ECO:0000269|PubMed:10049374};
CC Note=The values are approximate data due to the instability of the
CC substrate.;
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10049374};
CC Temperature dependence:
CC Optimum temperature is above 30 degrees Celsius. Heating to 60
CC degrees Celsius for 1 minute abolishes 72% of the original mutase
CC activity, and no activity remains after 8 minutes.
CC {ECO:0000269|PubMed:10049374};
CC -!- MISCELLANEOUS: 3HAP mutase requires neither a cofactor nor oxygen for
CC the enzymatic reaction. This indicates that the enzyme catalyzes a
CC Bamberger-type rearrangement.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; CP000090; AAZ61421.1; -; Genomic_DNA.
DR RefSeq; WP_011298219.1; NC_007347.1.
DR AlphaFoldDB; Q46ZL2; -.
DR SMR; Q46ZL2; -.
DR STRING; 264198.Reut_A2057; -.
DR PRIDE; Q46ZL2; -.
DR EnsemblBacteria; AAZ61421; AAZ61421; Reut_A2057.
DR KEGG; reu:Reut_A2057; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_2_4; -.
DR OMA; PHPHEFE; -.
DR OrthoDB; 416474at2; -.
DR BioCyc; MetaCyc:MON-15839; -.
DR GO; GO:0034022; F:3-(hydroxyamino)phenol mutase activity; IDA:UniProtKB.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR GO; GO:0042537; P:benzene-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR004809; Gln_synth_I.
DR InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10049374"
FT CHAIN 2..471
FT /note="3-hydroxylaminophenol mutase"
FT /id="PRO_0000418646"
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 107..471
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 471 AA; 52494 MW; 8B3B55E47D7857F1 CRC64;
MAQSVADVMK LVKENDVKFV DFRFTDTKGK EQHVSVPTSH FDDDKFESGH AFDGSSIAGW
KGIEASDMLL MPDSNTAFID PFYEEPTLVL TCDVVEPSDG KGYDRDPRSI AKRAEAYLKS
TGLGDTAFFG PEPEFFIFDG VTWNVDMQGC FVKVHSEEAP WSSGKEFEHG NSGHRPGKKG
GYFPVAPIDT FQDMRSEMCL ILESLGIPVE VHHHEVAGQG QNEIGTRFST LVQRADWTQL
QKYVIQNVAH TYGKTATFMP KPIVGDNGSG MHVHQSVWKD GQNLFAGNGY AGLSEFALYY
IGGIIKHARA LNAITNPGTN SYKRLVPGFE APVKLAYSAR NRSASIRIPY VANPKGRRIE
TRFPDPLMNP YLGFSALLMA GLDGVMNKIH PGEAADKNLY DLPPEEDAKI PTVCNSLDQS
LEYLDNDREF LTRGGVFSNS MLDAYIELKM EEVTRFRMTT HPVEFEMYYS L
