ID Q5QXQ5_IDILO Unreviewed; 177 AA.
AC Q5QXQ5;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN Name=fldA {ECO:0000313|EMBL:AAV82315.1};
GN OrderedLocusNames=IL1475 {ECO:0000313|EMBL:AAV82315.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82315.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82315.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC {ECO:0000256|PIRNR:PIRNR038996}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR038996};
CC -!- SIMILARITY: Belongs to the flavodoxin family.
CC {ECO:0000256|ARBA:ARBA00005267, ECO:0000256|PIRNR:PIRNR038996}.
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DR EMBL; AE017340; AAV82315.1; -; Genomic_DNA.
DR RefSeq; WP_011234721.1; NC_006512.1.
DR AlphaFoldDB; Q5QXQ5; -.
DR STRING; 283942.IL1475; -.
DR KEGG; ilo:IL1475; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_1_1_6; -.
DR OrthoDB; 359268at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR010086; Flavodoxin_lc.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR NCBIfam; TIGR01752; flav_long; 1.
DR PANTHER; PTHR42809:SF1; FLAVODOXIN 1; 1.
DR PANTHER; PTHR42809; FLAVODOXIN 2; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PIRSF; PIRSF038996; FldA; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|PIRNR:PIRNR038996};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR038996};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR038996};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT DOMAIN 4..165
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 177 AA; 19959 MW; 901B568EAD307D8E CRC64;
MATVGIFFGS DTGNTEAVAQ MIQKELGKKL VDVKDIAKSS KEDIANYDLL LFGIPTWYYG
EAQCDWDDFF PELEEIDFTD KLIAIFGCGD QEDYAEYFLD AMGMVRDIVE ARGGIIVGHW
PTESYNFEAS KGMADDTHFV GLGIDEDRQP ELTKERVSKW CQQVYEEMCL AELASDS
//
