FDR_SPHSX
ID FDR_SPHSX Reviewed; 414 AA.
AC D5IGG6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Ferredoxin--NAD(P)(+) reductase fdr;
DE EC=1.18.1.2;
DE EC=1.18.1.3;
DE AltName: Full=Carbazole 1,9a-dioxygenase, ferredoxin reductase component;
DE Short=CARDO;
GN Name=fdr;
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 {ECO:0000269|PubMed:20368802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; GU123624; ADC31800.1; -; Genomic_DNA.
DR AlphaFoldDB; D5IGG6; -.
DR SMR; D5IGG6; -.
DR BioCyc; MetaCyc:MON-15739; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; ISS:UniProtKB.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0046232; P:carbazole catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; NAD; NADP; Oxidoreductase.
FT CHAIN 1..414
FT /note="Ferredoxin--NAD(P)(+) reductase fdr"
FT /id="PRO_0000419027"
FT BINDING 7..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 149..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 414 AA; 44250 MW; 8A4DFCC73A4F2C16 CRC64;
MTDTHYDVVI VGAGHGGAQT AIALRQNGFA GTIAIIGAEP DLPYERPPLS KEYLAAEKGF
ERILIRPASF WNDRHIAMHL GCAVERVDPT QRLVFLADGR SMGYGDLVWC AGGSARRLDC
TGHDLGGVHY VRTRADTDAL AAELPGVSKV VIIGGGYIGL EAAAVMAKFG KNVTLIEALD
RVLARVAGEP LSRFFEEKHR SRGVDVRLRT KVGCLLGQDG RVTHVELNDA DPIPADLVIV
GIGIIPAISP LVVAGAKASN GLLVDASGRT SIPHVYALGD CAAHVNSFAP NDIPIRLESV
QNANDQAVVV ARTICGTAAQ YHAVPWFWSS QYDIRLQTVG LTAGYDQTFV RGDPATGSFT
VVYGRDGRVI ALDCVNATKD YVQGKRLVEA KALIEPGMTD PQYPLKNFMT PSPA
