FMNRE_PSEAE
ID FMNRE_PSEAE Reviewed; 185 AA.
AC Q9I4D4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=NAD(P)H-dependent FMN reductase PA1204 {ECO:0000303|PubMed:16552139};
DE EC=1.-.-.- {ECO:0000269|PubMed:16552139};
GN OrderedLocusNames=PA1204 {ECO:0000312|EMBL:AAG04593.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000312|EMBL:AAG04593.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:1RTT, ECO:0007744|PDB:1X77}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 2-181 OF APO FORM AND HOLO FORM
RP IN COMPLEX WITH FMN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16552139; DOI=10.1107/s0907444906001600;
RA Agarwal R., Bonanno J.B., Burley S.K., Swaminathan S.;
RT "Structure determination of an FMN reductase from Pseudomonas aeruginosa
RT PA01 using sulfur anomalous signal.";
RL Acta Crystallogr. D 62:383-391(2006).
CC -!- FUNCTION: Has NAD(P)H-dependent FMN reductase activity.
CC {ECO:0000269|PubMed:16552139}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16552139};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16552139}.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG04593.1; -; Genomic_DNA.
DR PIR; H83495; H83495.
DR RefSeq; NP_249895.1; NC_002516.2.
DR RefSeq; WP_003082483.1; NZ_QZGE01000006.1.
DR PDB; 1RTT; X-ray; 1.28 A; A=2-181.
DR PDB; 1X77; X-ray; 2.70 A; A/B=2-181.
DR PDBsum; 1RTT; -.
DR PDBsum; 1X77; -.
DR AlphaFoldDB; Q9I4D4; -.
DR SMR; Q9I4D4; -.
DR STRING; 287.DR97_730; -.
DR PaxDb; Q9I4D4; -.
DR PRIDE; Q9I4D4; -.
DR DNASU; 882133; -.
DR EnsemblBacteria; AAG04593; AAG04593; PA1204.
DR GeneID; 882133; -.
DR KEGG; pae:PA1204; -.
DR PATRIC; fig|208964.12.peg.1250; -.
DR PseudoCAP; PA1204; -.
DR HOGENOM; CLU_055322_4_2_6; -.
DR InParanoid; Q9I4D4; -.
DR OMA; YGGVWAQ; -.
DR PhylomeDB; Q9I4D4; -.
DR BioCyc; PAER208964:G1FZ6-1229-MON; -.
DR EvolutionaryTrace; Q9I4D4; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IMP:PseudoCAP.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:PseudoCAP.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..185
FT /note="NAD(P)H-dependent FMN reductase PA1204"
FT /id="PRO_0000431994"
FT BINDING 13..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16552139"
FT BINDING 81..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16552139"
FT BINDING 115..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:16552139"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1RTT"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1RTT"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1RTT"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1RTT"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1X77"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:1RTT"
SQ SEQUENCE 185 AA; 20224 MW; FED24F33D526D37A CRC64;
MSDDIKVLGI SGSLRSGSYN SAALQEAIGL VPPGMSIELA DISGIPLYNE DVYALGFPPA
VERFREQIRA ADALLFATPE YNYSMAGVLK NAIDWASRPP EQPFSGKPAA ILGASAGRFG
TARAQYHLRQ TLVFLDVHPL NKPEVMISSA QNAFDAQGRL LDDKARELIQ QQLQALQLWV
RRLRG
