ABSAB_ALCSP
ID ABSAB_ALCSP Reviewed; 150 AA.
AC Q9RBG4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=2-aminobenzenesulfonate 2,3-dioxygenase subunit beta {ECO:0000303|PubMed:10589735};
DE EC=1.14.12.14 {ECO:0000269|PubMed:10589735};
DE AltName: Full=2-aminobenzenesulfonate dioxygenase small subunit {ECO:0000312|EMBL:AAF14228.2};
DE AltName: Full=AbsAb {ECO:0000312|EMBL:AAF14228.2};
GN Name=absAb {ECO:0000303|PubMed:10589735};
OS Alcaligenes sp.
OG Plasmid pSAH {ECO:0000312|EMBL:AAF14228.2}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=512;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O-1 {ECO:0000312|EMBL:AAF14228.2}; PLASMID=pSAH;
RX PubMed=19577910; DOI=10.1016/j.micres.2009.05.006;
RA Ruff J., Smits T.H., Cook A.M., Schleheck D.;
RT "Identification of two vicinal operons for the degradation of 2-
RT aminobenzenesulfonate encoded on plasmid pSAH in Alcaligenes sp. strain O-
RT 1.";
RL Microbiol. Res. 165:288-299(2010).
RN [2]
RP PROTEIN SEQUENCE OF 1-28, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=O-1 {ECO:0000312|EMBL:AAF14228.2}; PLASMID=pSAH;
RX PubMed=10589735; DOI=10.1099/00221287-145-11-3255;
RA Mampel J., Ruff J., Junker F., Cook A.M.;
RT "The oxygenase component of the 2-aminobenzenesulfonate dioxygenase system
RT from Alcaligenes sp. strain O-1.";
RL Microbiology 145:3255-3264(1999).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=8075807; DOI=10.1099/13500872-140-7-1713;
RA Junker F., Leisinger T., Cook A.M.;
RT "3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and
RT EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic,
RT benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-
RT 1.";
RL Microbiology 140:1713-1722(1994).
RN [4]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Beta subunit of the oxygenase component of the 2-
CC aminobenzenesulfonate 2,3-dioxygenase system (deaminating) (ABSDOS).
CC Can use 2-aminobenzenesulfonate (ABS), benzenesulfonate (BS), 4-
CC toluenesulfonate (TS), 2-nitrobenzenesulfonate, 3- and 4-
CC aminobenzenesulfonates, 4-chloro- and 4-hydroxybenzenesulfonates and
CC pyridine-3-sulfonate as substrates. No desulfonation of ABS to
CC aminocatechol or aminophenol detected. {ECO:0000269|PubMed:10589735,
CC ECO:0000269|PubMed:8075807}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-aminobenzenesulfonate + 2 H(+) + NADH + O2 = 2,3-
CC dihydroxybenzenesulfonate + NAD(+) + NH4(+); Xref=Rhea:RHEA:23468,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15942,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:33565, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.14;
CC Evidence={ECO:0000269|PubMed:10589735};
CC -!- ACTIVITY REGULATION: Inhibited by o-phenanthroline.
CC {ECO:0000269|PubMed:10589735}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for 2-aminobenzenesulfonate {ECO:0000269|PubMed:10589735};
CC KM=18 uM for benzenesulfonate {ECO:0000269|PubMed:10589735};
CC KM=108 uM for 4-toluenesulfonate {ECO:0000269|PubMed:10589735};
CC Vmax=140 pmol/sec/mg enzyme with 2-aminobenzenesulfonate as substrate
CC {ECO:0000269|PubMed:10589735};
CC Vmax=118 pmol/sec/mg enzyme with benzenesulfonate as substrate
CC {ECO:0000269|PubMed:10589735};
CC Vmax=72 pmol/sec/mg enzyme with 4-toluenesulfonate as substrate
CC {ECO:0000269|PubMed:10589735};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10589735};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:10589735};
CC -!- SUBUNIT: Heterotetramer with a alpha2beta2 structure.
CC {ECO:0000269|PubMed:10589735}.
CC -!- INDUCTION: Part of the abs operon that is induced during growth with 2-
CC aminobenzenesulfonate (ABS) as carbon source.
CC {ECO:0000269|PubMed:10589735, ECO:0000269|PubMed:8075807}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC beta subunit family. {ECO:0000305}.
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DR EMBL; AF109074; AAF14228.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9RBG4; -.
DR SMR; Q9RBG4; -.
DR KEGG; ag:AAF14228; -.
DR BRENDA; 1.14.12.14; 10863.
DR GO; GO:0018627; F:2-aminobenzenesulfonate 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..150
FT /note="2-aminobenzenesulfonate 2,3-dioxygenase subunit
FT beta"
FT /id="PRO_0000430787"
FT CONFLICT 11
FT /note="Y -> W (in Ref. 2; AA sequence)"
FT CONFLICT 25
FT /note="W -> G (in Ref. 2; AA sequence)"
SQ SEQUENCE 150 AA; 17220 MW; 1EDE9A4A72AD198D CRC64;
MDTVSIAEFL YTNADLLNQE QFDSWLEQCS NDFSYRITTF SEELGRPMDW MDKDKSGLAH
YLQNANNHER YTGRLRRHLA MPRVTKQADS SFEVRTAVAI YVIEMNGETA LYGIGSYVDN
VMSESSGLRL TSRVVTLDTR RLQFGPHVPI
