ID   CINC_CITBR              Reviewed;         154 AA.
AC   Q8VQF4;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cindoxin;
DE            Short=Cdx;
DE   AltName: Full=FMN-containing redox partner;
GN   Name=cinC;
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].
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).
RN   [2]
RP   FUNCTION.
RX   PubMed=17606612; DOI=10.1074/jbc.m703790200;
RA   Kimmich N., Das A., Sevrioukova I., Meharenna Y., Sligar S.G., Poulos T.L.;
RT   "Electron transfer between cytochrome P450cin and its FMN-containing redox
RT   partner, cindoxin.";
RL   J. Biol. Chem. 282:27006-27011(2007).
RN   [3]
RP   FUNCTION, COFACTOR, MASS SPECTROMETRY, AND REACTION MECHANISM.
RX   PubMed=20419722; DOI=10.1002/cbic.201000119;
RA   Hawkes D.B., Slessor K.E., Bernhardt P.V., De Voss J.J.;
RT   "Cloning, expression and purification of cindoxin, an unusual Fmn-
RT   containing cytochrome p450 redox partner.";
RL   ChemBioChem 11:1107-1114(2010).
CC   -!- FUNCTION: Involved in the degradation of cineol (eucalyptol). The FMN
CC       protein, cindoxin, shuttles electrons between the FAD-containing
CC       cindoxin reductase (CinB) and 1,8-cineole 2-endo-monooxygenase (CinA).
CC       {ECO:0000269|PubMed:17606612, ECO:0000269|PubMed:20419722}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:20419722};
CC   -!- MASS SPECTROMETRY: Mass=15964; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20419722};
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; AF456128; AAL57616.1; -; Genomic_DNA.
DR   PDB; 4OXX; X-ray; 1.21 A; A=1-154.
DR   PDBsum; 4OXX; -.
DR   AlphaFoldDB; Q8VQF4; -.
DR   SMR; Q8VQF4; -.
DR   BioCyc; MetaCyc:MON-17204; -.
DR   GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN           1..154
FT                   /note="Cindoxin"
FT                   /id="PRO_0000422768"
FT   DOMAIN          3..145
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         9..13
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000305"
FT   BINDING         89..120
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           13..25
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          50..59
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           102..113
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:4OXX"
FT   HELIX           133..148
FT                   /evidence="ECO:0007829|PDB:4OXX"
SQ   SEQUENCE   154 AA;  15966 MW;  AB2CCF3000AC4D31 CRC64;
     MNALILYGTE TGNAEACATT ISQVLADTVD TKVHDLADMT PRAMLDSGAD LIVFATATYG
     EGEFAGGGAA FFETLRETKP DLSGLRFAVF GLGDSYYTTF NQAGATAATI LASLGGTQVG
     DTARHDTSSG DDPEETAEEW AREILTALAT PAVS