(data stored in SCRATCH zone)

SWISSPROT: Q3ILE2_PSEHT

ID   Q3ILE2_PSEHT            Unreviewed;       173 AA.
AC   Q3ILE2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 73.
DE   RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN   Name=fldB {ECO:0000313|EMBL:CAI85603.1};
GN   OrderedLocusNames=PSHAa0513 {ECO:0000313|EMBL:CAI85603.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85603.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85603.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. {ECO:0000256|PIRNR:PIRNR038996}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038996};
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC       {ECO:0000256|PIRNR:PIRNR038996}.
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DR   EMBL; CR954246; CAI85603.1; -; Genomic_DNA.
DR   RefSeq; WP_011327216.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILE2; -.
DR   STRING; 326442.PSHAa0513; -.
DR   EnsemblBacteria; CAI85603; CAI85603; PSHAa0513.
DR   KEGG; pha:PSHAa0513; -.
DR   PATRIC; fig|326442.8.peg.482; -.
DR   eggNOG; ENOG41071R3; Bacteria.
DR   eggNOG; COG0716; LUCA.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03840; -.
DR   OMA; ILGISTW; -.
DR   OrthoDB; POG091H029L; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 2.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   InterPro; IPR029039; Flavoprotein-like_dom.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PIRSF; PIRSF038996; FldA; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILE2.
DR   SWISS-2DPAGE; Q3ILE2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR038996};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR038996};
KW   FMN {ECO:0000256|PIRNR:PIRNR038996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transport {ECO:0000256|PIRNR:PIRNR038996}.
FT   DOMAIN        3    166       Flavodoxin-like. {ECO:0000259|PROSITE:
FT                                PS50902}.
SQ   SEQUENCE   173 AA;  19752 MW;  4AF8E1531475138D CRC64;
     MQIGLFFGST TCYTEMAAEK IRDIIGADIV TLHNIKDEPL KNAEQYDFII FGISTWDFGE
     IQEDWESKWD DIADVNLNGK TIALFGMGDQ QGYGQWFQDA LGMLHDEISP QTFTQLGFWP
     NDNSYEFEAS KALTEDGTHF VGLALDEDSQ YELSDERIAT WVEQVMTEYS ETL
//

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