ID B2RLR5_PORG3 Unreviewed; 165 AA.
AC B2RLR5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN OrderedLocusNames=PGN_1791 {ECO:0000313|EMBL:BAG34310.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG34310.1, ECO:0000313|Proteomes:UP000008842};
RN [1] {ECO:0000313|EMBL:BAG34310.1, ECO:0000313|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC 2561 {ECO:0000313|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG34310.1; -; Genomic_DNA.
DR RefSeq; WP_005874342.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RLR5; -.
DR SMR; B2RLR5; -.
DR GeneID; 29256948; -.
DR KEGG; pgn:PGN_1791; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_1_0_10; -.
DR OrthoDB; 9790745at2; -.
DR BioCyc; PGIN431947:G1G2V-2002-MONOMER; -.
DR Proteomes; UP000008842; Chromosome.
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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT DOMAIN 4..164
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 165 AA; 17195 MW; FB11F4E6BCA59B0D CRC64;
MKSIGIFYGS STGTTSDLAQ KIASALGVDS ANVMDVANAD AAAAAKYDVL LLGSSTWGLG
DLQDDWESFL PKLKGENLSG KKVGLFGCGD ASSYSDTFCA ALGTIKAELA NTGCTFIGAY
PAEGYSYDET TAEENGQLIG LCVDDANESD QTEARMERWI AAMGL
//