SSUE_ECOLI
ID SSUE_ECOLI Reviewed; 191 AA.
AC P80644; P75854;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=FMN reductase (NADPH);
DE EC=1.5.1.38;
DE AltName: Full=FMN reductase;
DE AltName: Full=Sulfate starvation-induced protein 4;
DE Short=SSI4;
GN Name=ssuE; Synonyms=ycbP; OrderedLocusNames=b0937, JW0920;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10506196; DOI=10.1074/jbc.274.41.29358;
RA Van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M.M.,
RA Leisinger T.;
RT "The Escherichia coli ssuEADCB gene cluster is required for the utilization
RT of sulfur from aliphatic sulfonates and is regulated by the transcriptional
RT activator Cbl.";
RL J. Biol. Chem. 274:29358-29365(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-14.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10480865; DOI=10.1074/jbc.274.38.26639;
RA Eichhorn E., van der Ploeg J.R., Leisinger T.;
RT "Characterization of a two-component alkanesulfonate monooxygenase from
RT Escherichia coli.";
RL J. Biol. Chem. 274:26639-26646(1999).
CC -!- FUNCTION: Catalyzes an NADPH-dependent reduction of FMN, but is also
CC able to reduce FAD or riboflavin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.38;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P80644; P80645: ssuD; NbExp=2; IntAct=EBI-1121047, EBI-561637;
CC -!- INDUCTION: Repressed by sulfate or cysteine.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; AJ237695; CAB40389.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74023.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35692.1; -; Genomic_DNA.
DR PIR; H64833; H64833.
DR RefSeq; NP_415457.1; NC_000913.3.
DR RefSeq; WP_001263933.1; NZ_STEB01000006.1.
DR PDB; 4PTY; X-ray; 2.10 A; A/B/C/D=1-191.
DR PDB; 4PTZ; X-ray; 1.90 A; A/B/C/D=1-191.
DR PDB; 4PU0; X-ray; 2.30 A; A/B/C/D=1-191.
DR PDB; 6DQI; X-ray; 1.95 A; A/B=1-191.
DR PDB; 6DQO; X-ray; 1.71 A; A=1-191.
DR PDB; 6DQP; X-ray; 1.55 A; A/B=1-191.
DR PDBsum; 4PTY; -.
DR PDBsum; 4PTZ; -.
DR PDBsum; 4PU0; -.
DR PDBsum; 6DQI; -.
DR PDBsum; 6DQO; -.
DR PDBsum; 6DQP; -.
DR AlphaFoldDB; P80644; -.
DR SMR; P80644; -.
DR BioGRID; 4262118; 30.
DR BioGRID; 850311; 1.
DR ComplexPortal; CPX-2118; FMN reductase complex.
DR DIP; DIP-10929N; -.
DR IntAct; P80644; 5.
DR STRING; 511145.b0937; -.
DR PaxDb; P80644; -.
DR PRIDE; P80644; -.
DR EnsemblBacteria; AAC74023; AAC74023; b0937.
DR EnsemblBacteria; BAA35692; BAA35692; BAA35692.
DR GeneID; 945947; -.
DR KEGG; ecj:JW0920; -.
DR KEGG; eco:b0937; -.
DR PATRIC; fig|1411691.4.peg.1337; -.
DR EchoBASE; EB3472; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_3_0_6; -.
DR InParanoid; P80644; -.
DR OMA; DVEVCHW; -.
DR PhylomeDB; P80644; -.
DR BioCyc; EcoCyc:MON0-146; -.
DR BioCyc; MetaCyc:MON0-146; -.
DR BRENDA; 1.5.1.38; 2026.
DR PRO; PR:P80644; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990202; C:FMN reductase complex; IDA:EcoCyc.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008752; F:FMN reductase activity; IDA:EcoCyc.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IDA:ComplexPortal.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP:EcoCyc.
DR DisProt; DP01735; -.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR020048; NADPH-dep_FMN_reduc_SsuE.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR03567; FMN_reduc_SsuE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..191
FT /note="FMN reductase (NADPH)"
FT /id="PRO_0000160591"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:6DQP"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6DQP"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6DQP"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6DQP"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:6DQP"
SQ SEQUENCE 191 AA; 21253 MW; 2371808C97CEE532 CRC64;
MRVITLAGSP RFPSRSSSLL EYAREKLNGL DVEVYHWNLQ NFAPEDLLYA RFDSPALKTF
TEQLQQADGL IVATPVYKAA YSGALKTLLD LLPERALQGK VVLPLATGGT VAHLLAVDYA
LKPVLSALKA QEILHGVFAD DSQVIDYHHR PQFTPNLQTR LDTALETFWQ ALHRRDVQVP
DLLSLRGNAH A
