ID   HABB_PSEOL              Reviewed;         164 AA.
AC   O52216;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Hydroxylaminobenzene mutase HabB;
DE            Short=HAB mutase;
DE            EC=5.4.4.1;
DE   AltName: Full=(Hydroxyamino)benzene mutase;
GN   Name=habB;
OS   Pseudomonas oleovorans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=JS45;
RX   PubMed=10877793; DOI=10.1128/aem.66.7.2965-2971.2000;
RA   Davis J.K., Paoli G.C., He Z., Nadeau L.J., Somerville C.C., Spain J.C.;
RT   "Sequence analysis and initial characterization of two isozymes of
RT   hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45.";
RL   Appl. Environ. Microbiol. 66:2965-2971(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=JS45;
RX   PubMed=10672020; DOI=10.1046/j.1432-1327.2000.01107.x;
RA   He Z., Nadeau L.J., Spain J.C.;
RT   "Characterization of hydroxylaminobenzene mutase from pNBZ139 cloned from
RT   Pseudomonas pseudoalcaligenes JS45. A highly associated SDS-stable enzyme
RT   catalyzing an intramolecular transfer of hydroxy groups.";
RL   Eur. J. Biochem. 267:1110-1116(2000).
CC   -!- FUNCTION: Catalyzes the rearrangement of hydroxylaminobenzene to 2-
CC       aminophenol. {ECO:0000269|PubMed:10672020,
CC       ECO:0000269|PubMed:10877793}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-phenylhydroxylamine = 2-aminophenol; Xref=Rhea:RHEA:19245,
CC         ChEBI:CHEBI:18112, ChEBI:CHEBI:28902; EC=5.4.4.1;
CC         Evidence={ECO:0000269|PubMed:10672020, ECO:0000269|PubMed:10877793};
CC   -!- ACTIVITY REGULATION: Addition of ZnSO(4) decreases the activity to 70%.
CC       {ECO:0000269|PubMed:10672020}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.15 mM for hydroxylaminobenzene (at pH 7)
CC         {ECO:0000269|PubMed:10672020};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Could be membrane-associated.
CC       {ECO:0000269|PubMed:10877793}.
CC   -!- DISRUPTION PHENOTYPE: Mutants can still grow on nitrobenzene.
CC       {ECO:0000269|PubMed:10877793}.
CC   -!- MISCELLANEOUS: Not expressed in strain JS45 under standard conditions,
CC       but is functional when expressed in E.coli.
CC       {ECO:0000305|PubMed:10877793}.
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DR   EMBL; AF028594; AAB94123.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52216; -.
DR   SMR; O52216; -.
DR   KEGG; ag:AAB94123; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0018824; F:(hydroxyamino)benzene mutase activity; IEA:RHEA.
PE   1: Evidence at protein level;
KW   Cell membrane; Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..164
FT                   /note="Hydroxylaminobenzene mutase HabB"
FT                   /id="PRO_0000418543"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   164 AA;  16955 MW;  EA10D79B837B3B29 CRC64;
     MTLHTPSTDA PLARRLLQLG IALFLLGLLT GFLLPMMANP RVGLSSHLEG VLNGMFLLAL
     GLMWPQLSLG TGARKAAFGF AVYGTYANWL ATLLAGFWGA GGRMMPIAAG GHTGTAAQEG
     LIAFALISLS LSMLVVCALA LWGLRSAPAR RNTDAPAAGP QPAA