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Database: UniProt
Entry: A8TAF7_9VIBR
LinkDB: A8TAF7_9VIBR
Original site: A8TAF7_9VIBR 
ID   A8TAF7_9VIBR            Unreviewed;       172 AA.
AC   A8TAF7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN   ORFNames=AND4_19012 {ECO:0000313|EMBL:EDP57684.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP57684.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP57684.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP57684.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC       {ECO:0000256|ARBA:ARBA00003297, 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP57684.1}.
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DR   EMBL; ABGR01000026; EDP57684.1; -; Genomic_DNA.
DR   RefSeq; WP_009844008.1; NZ_ABGR01000026.1.
DR   AlphaFoldDB; A8TAF7; -.
DR   OrthoDB; 359268at2; -.
DR   Proteomes; UP000005159; Unassembled WGS sequence.
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; FLAVODOXIN 2; 1.
DR   PANTHER; PTHR42809:SF3; 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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT   DOMAIN          3..165
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   172 AA;  19505 MW;  06265A475FCDC2FE CRC64;
     MKIGLFYGST TCYTEMAAEK IRNIIGEDLV DIHNVKETPL SLMADYDLLL IGISTWDFGE
     IQEDWSAIWE DIAITPLKGK VVALFGLGDQ EGYGEWYLDA MGLLHDELKV TGVQFIGYWP
     NEGYEFEASK ALSEDGSQFV GLALDEDSQY ELSDERIEKW CEQVLVEFHD TL
//
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