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Database: UniProt
Entry: A0A3P1Z3J6_9BACT
LinkDB: A0A3P1Z3J6_9BACT
Original site: A0A3P1Z3J6_9BACT 
ID   A0A3P1Z3J6_9BACT        Unreviewed;       162 AA.
AC   A0A3P1Z3J6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN   ORFNames=EII14_07330 {ECO:0000313|EMBL:RRD77754.1};
OS   Alloprevotella sp. OH1205_COT-284.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=2491043 {ECO:0000313|EMBL:RRD77754.1, ECO:0000313|Proteomes:UP000272376};
RN   [1] {ECO:0000313|EMBL:RRD77754.1, ECO:0000313|Proteomes:UP000272376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH1205_COT-284 {ECO:0000313|EMBL:RRD77754.1,
RC   ECO:0000313|Proteomes:UP000272376};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RRD77754.1}.
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DR   EMBL; RQYI01000028; RRD77754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1Z3J6; -.
DR   OrthoDB; 9790745at2; -.
DR   Proteomes; UP000272376; 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   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR001094; Flavdoxin-like.
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   PRINTS; PR00369; FLAVODOXIN.
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|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR038996};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR038996};
KW   FMN {ECO:0000256|PIRNR:PIRNR038996};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272376};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT   DOMAIN          2..161
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   162 AA;  16717 MW;  6F525A36ADF219B4 CRC64;
     MTGIFYGSTT GNTEAAAQEI ASALGVSSDQ VYNVGEVGAD TVAQFDTLIL GSSTWGCGDL
     QDDWYDFLDQ LKAQDLSGKR IALFGCGDSD GYADTFCGAL AQIYDALADS GATFVGQVDA
     AGIAATDTEA CRDGKFVGLP IDDADPEGNA ARMAAWVESV KA
//
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