CARAC_SPHSX
ID CARAC_SPHSX Reviewed; 109 AA.
AC D5IGG4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Ferredoxin CarAc;
DE AltName: Full=Carbazole 1,9a-dioxygenase, ferredoxin component;
DE Short=CARDO;
GN Name=carAc;
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 Acts as a mediator in the electron transfer from fdr to CarAa.
CC {ECO:0000269|PubMed:20368802}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. 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}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; GU123624; ADC31798.1; -; Genomic_DNA.
DR AlphaFoldDB; D5IGG4; -.
DR SMR; D5IGG4; -.
DR BioCyc; MetaCyc:MON-15738; -.
DR BRENDA; 1.14.12.22; 5801.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0008901; F:ferredoxin hydrogenase 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 GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding.
FT CHAIN 1..109
FT /note="Ferredoxin CarAc"
FT /id="PRO_0000419029"
FT DOMAIN 3..108
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 109 AA; 11570 MW; 3BD54F264BFE7805 CRC64;
MTAKVRVIFR AAGGFEHLVE TEAGVSLMEA AVLNGVDGIE AVCGGACACA TCHVYVGPEW
LDALKPPSET EDEMLDCVAE RAPHSRLSCQ IRLTDLLDGL TLELPKAQS
