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Database: UniProt
Entry: A0A101HMY0_9BACT
LinkDB: A0A101HMY0_9BACT
Original site: A0A101HMY0_9BACT 
ID   A0A101HMY0_9BACT        Unreviewed;       144 AA.
AC   A0A101HMY0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN   ORFNames=XD95_0085 {ECO:0000313|EMBL:KUK79832.1};
OS   Microgenomates bacterium 39_7.
OC   Bacteria; Candidatus Microgenomates.
OX   NCBI_TaxID=1641390 {ECO:0000313|EMBL:KUK79832.1, ECO:0000313|Proteomes:UP000054437};
RN   [1] {ECO:0000313|Proteomes:UP000054437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK79832.1}.
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DR   EMBL; LGGQ01000005; KUK79832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101HMY0; -.
DR   PATRIC; fig|1641390.4.peg.580; -.
DR   Proteomes; UP000054437; 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   PANTHER; PTHR42809:SF1; FLAVODOXIN 1; 1.
DR   PANTHER; PTHR42809; FLAVODOXIN 2; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PIRSF; PIRSF038996; FldA; 2.
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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT   DOMAIN          4..141
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   144 AA;  15993 MW;  3671B9104ABF6404 CRC64;
     MAKILIVYGS TTGNTEMVAE QIMDLLEESS PELQDVADIN PEDFGKYDLL IMGSSTWDDG
     LLQADFRDFV NNNELDLSGK KVAVFGLGDS SYPDFCEAAT LLEEVVNKSG GELLLESLKL
     DGFPDEEENE EKIKVWCSNI KKKM
//
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