ABSAA_ALCSP
ID ABSAA_ALCSP Reviewed; 394 AA.
AC Q9RBG5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=2-aminobenzenesulfonate 2,3-dioxygenase subunit alpha {ECO:0000303|PubMed:10589735};
DE EC=1.14.12.14 {ECO:0000269|PubMed:10589735};
DE AltName: Full=2-aminobenzenesulfonate dioxygenase large subunit {ECO:0000312|EMBL:AAF14227.2};
DE AltName: Full=AbsAa {ECO:0000312|EMBL:AAF14227.2};
GN Name=absAa {ECO:0000303|PubMed:10589735};
OS Alcaligenes sp.
OG Plasmid pSAH {ECO:0000312|EMBL:AAF14227.2}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=512;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVITY
RP REGULATION, AND INDUCTION.
RC STRAIN=O-1 {ECO:0000312|EMBL:AAF14227.2}; 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O-1 {ECO:0000312|EMBL:AAF14227.2}; 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 [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: Alpha 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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:10589735};
CC Note=Binds 1 Fe cation per subunit. {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 alpha subunit family. {ECO:0000305}.
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DR EMBL; AF109074; AAF14227.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9RBG5; -.
DR SMR; Q9RBG5; -.
DR KEGG; ag:AAF14227; -.
DR BRENDA; 1.14.12.14; 10863.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018627; F:2-aminobenzenesulfonate 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Dioxygenase; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000303|PubMed:10589735"
FT CHAIN 2..394
FT /note="2-aminobenzenesulfonate 2,3-dioxygenase subunit
FT alpha"
FT /id="PRO_0000430788"
FT DOMAIN 43..154
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q7N4W0"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q7N4W0"
SQ SEQUENCE 394 AA; 45885 MW; 9C6E2578E300BA8B CRC64;
MSRSAAEFLK PQNVASTHYL DNRVYWDHEI FEEEKKRIFS KVWKFVCHVS EIPSTFDYRT
IKVADTPLVV IRGKDEKVRT FVNACSHRGI QIVRRPRGNA KTMECIFHRW NYDSTNGELT
GAPRKEAYGP SNFDLKQCGL REVRTETYLG LVFVNLDDSA VSLSEFIGDA LEMEKDILGA
EELEVFDYYE QVLDTNWKNW QETNLDLYHE FMHFANRKTG LTVKEYYQRA WKLYPNGHAA
IERYRAQYSN YAGWQDRDDG IRLPGLHPNE FQLVNLFPDL AINARGTVIR IDSQTPISPG
KTLVQYRGLG LKRDSERERV QRVRDYTSIW GPFGTNLAED TLATSLHAKT IQTGSVPFTY
LTRDEGGMTQ DDLGLRTFYR EWERLMSRQA NQIR
