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Database: UniProt
Entry: Q87RG2_VIBPA
LinkDB: Q87RG2_VIBPA
Original site: Q87RG2_VIBPA 
ID   Q87RG2_VIBPA            Unreviewed;       177 AA.
AC   Q87RG2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN   OrderedLocusNames=VP0835 {ECO:0000313|EMBL:BAC59098.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59098.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59098.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC59098.1; -; Genomic_DNA.
DR   RefSeq; NP_797214.1; NC_004603.1.
DR   RefSeq; WP_005489824.1; NC_004603.1.
DR   AlphaFoldDB; Q87RG2; -.
DR   GeneID; 1188332; -.
DR   KEGG; vpa:VP0835; -.
DR   PATRIC; fig|223926.6.peg.791; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_1_1_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
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:UP000002493};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT   DOMAIN          4..167
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   177 AA;  19849 MW;  FC1E030693B4B6EA CRC64;
     MASVGIFFGS DTGNTEAVAK MIQKQLGKHL VHVQDIAKSS KEDIDNFDLL LLGIPTWYYG
     EAQCDWDDFF PELEQIDFST KLVAIFGCGD QEDYAEYFCD AMGTVRDIVE SKGGTILGHT
     STEGYEFEAS KALVEGDDSQ FVGLCIDEDR QPELTDQRVE NWVKQIYEEM CLAELEG
//
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