CINB_CITBR
ID CINB_CITBR Reviewed; 451 AA.
AC Q8VQF5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cindoxin reductase;
DE Short=CdR;
DE EC=1.18.1.-;
DE AltName: Full=NADPH-dependent flavodoxin/ferredoxin reductase {ECO:0000305};
DE AltName: Full=NADPH-dependent flavodoxin/ferrodoxin reductase {ECO:0000303|PubMed:12016226};
GN Name=cinB;
OS Citrobacter braakii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=57706;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12016226; DOI=10.1074/jbc.m203382200;
RA Hawkes D.B., Adams G.W., Burlingame A.L., Ortiz de Montellano P.R.,
RA De Voss J.J.;
RT "Cytochrome P450(cin) (CYP176A), isolation, expression, and
RT characterization.";
RL J. Biol. Chem. 277:27725-27732(2002).
CC -!- FUNCTION: Involved in the degradation of cineol (eucalyptol). Catalyzes
CC the reduction of cindoxin (CinC). {ECO:0000269|PubMed:12016226}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: The authors of PubMed:12016226 consistently use the word
CC ferrodoxin instead of ferredoxin. {ECO:0000305}.
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DR EMBL; AF456128; AAL57615.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VQF5; -.
DR SMR; Q8VQF5; -.
DR BioCyc; MetaCyc:MON-17203; -.
DR GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase; Transport.
FT CHAIN 1..451
FT /note="Cindoxin reductase"
FT /id="PRO_0000422769"
FT BINDING 24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 345..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 49413 MW; 8403EA5D2F51E4D9 CRC64;
MSKLQHHSIG EVEPSIAIVG SGPAGCYTAQ TLHKQWPSAQ IVIFERLPVP YGLLRYGVSP
DHQGTKAIAR QFDRLFAEAS VHFIGNVEVG KHISVEELQD AFDVVVLAAG LGADRPLPSL
AGDAVYGAGQ VMRWFNSHPD EQSFAPGFGA TTTIIGNGNV AMDVVRLLAK HRDSFTGSDL
DPQLIEKQPS RIHVVGRSPA SAAKFDSMMI RELAEIDDAV FDVDVVDEPG HEDKRIHAKT
KALLDLTAAR AVPSPRVHVS FHFGWTPESL EPTGDGRTLR LVNTESRLAV KLIETDSVIT
AVGFGSGLRH EIDRVRFESA ASDLDNGLLD TGLYCSGWFR RGPTGGIPAN RLDAKMVCTR
IIEDVASGAI TPKKRGLEEL ATHLHPDTVD FTGWQRIDAV EASRTEHGRC RTKLPDIATM
LDFARNRTHE RTTDDTYRKQ ITDTVGHKEK R