CARAA_SPHSX
ID CARAA_SPHSX Reviewed; 378 AA.
AC D5IGG0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Carbazole 1,9a-dioxygenase, terminal oxygenase component CarAa;
DE Short=CARDO;
DE EC=1.14.12.22;
GN Name=carAa;
OS Sphingomonas sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28214;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN THE CARBAZOLE DEGRADATION,
RP AND NOMENCLATURE.
RC STRAIN=XLDN2-5;
RX PubMed=20368802; DOI=10.1371/journal.pone.0010018;
RA Gai Z., Wang X., Liu X., Tai C., Tang H., He X., Wu G., Deng Z., Xu P.;
RT "The genes coding for the conversion of carbazole to catechol are flanked
RT by IS6100 elements in Sphingomonas sp. strain XLDN2-5.";
RL PLoS ONE 5:E10018-E10018(2010).
CC -!- FUNCTION: Part of the multicomponent carbazole 1,9a-dioxygenase
CC (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
CC Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1)
CC positions of carbazole to yield a highly unstable cis-hydrodiol
CC intermediate which is spontaneously converted to 2-aminobiphenyl-2,3-
CC diol. {ECO:0000269|PubMed:20368802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9H-carbazole + H(+) + NADH + O2 = 2'-aminobiphenyl-2,3-diol +
CC NAD(+); Xref=Rhea:RHEA:27838, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27543, ChEBI:CHEBI:29010, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9H-carbazole + H(+) + NADPH + O2 = 2'-aminobiphenyl-2,3-diol +
CC NADP(+); Xref=Rhea:RHEA:27842, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27543, ChEBI:CHEBI:29010, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.12.22;
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 -!- SUBUNIT: Homotrimer. Carbazole 1,9a-dioxygenase complex consists of a
CC terminal oxygenase component CarAa, a ferredoxin reductase component
CC fdr and a ferredoxin component CarAc (Probable). {ECO:0000305}.
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DR EMBL; GU123624; ADC31794.1; -; Genomic_DNA.
DR AlphaFoldDB; D5IGG0; -.
DR SMR; D5IGG0; -.
DR KEGG; ag:ADC31794; -.
DR BioCyc; MetaCyc:MON-15737; -.
DR BRENDA; 1.14.12.22; 5801.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0018564; F:carbazole 1,9a-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046232; P:carbazole catabolic process; IDA:UniProtKB.
DR InterPro; IPR021028; Homotrim_ring_OHase_catalytic.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF11723; Aromatic_hydrox; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; NADP;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..378
FT /note="Carbazole 1,9a-dioxygenase, terminal oxygenase
FT component CarAa"
FT /id="PRO_0000419025"
FT DOMAIN 29..135
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 90
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 378 AA; 42626 MW; EACEEAE7DE931BCE CRC64;
MANQPSIAER RTKVWEPYIR AKLGFRNHWY PVRLASEIAE GTPVPVKLLG EKILLNRVGG
KVYAIQDRCL HRGVTLSDRV ECYSKNTISC WYHGWTYRWD DGRLVDILTN PGSVQIGRRA
LKTFPVEEAK GLIFVYVGDG EPTPLIEDVP PGFLDENRAI HGQHRLVASN WRLGAENGFD
AGHVLIHKNS ILVKGNDIIL PLGFAPGDPD QLTRSEVAAG KPKGVYDLLG EHSVPVFEGM
IEGKPAIHGN IGSKRVAISI SIWLPGVLKV EPWPDPELTQ FEWYVPVDET SHLYFQTLGK
VVTSKEAADS FEREFHEKWV GLALNGFNDD DIMARESMEP FYTDDRGWSE EILFEPDRAI
IEWRGLASQH NRGIQEAR
