ID   FLAV_RHOCB              Reviewed;         182 AA.
AC   P52967; D5AT59;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 3.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Flavodoxin;
GN   Name=nifF; Synonyms=fldA; OrderedLocusNames=RCAP_rcc01421;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=8682802; DOI=10.1128/jb.178.13.3949-3952.1996;
RA   Gennaro G., Huebner P., Sandmeier U., Yakunin A.F., Hallenbeck P.C.;
RT   "Cloning, characterization, and regulation of nifF from Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 178:3949-3952(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC       NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; L42290; AAC05792.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85166.1; -; Genomic_DNA.
DR   RefSeq; WP_013067145.1; NC_014034.1.
DR   PDB; 2WC1; X-ray; 2.17 A; A=1-182.
DR   PDBsum; 2WC1; -.
DR   AlphaFoldDB; P52967; -.
DR   SMR; P52967; -.
DR   STRING; 272942.RCAP_rcc01421; -.
DR   EnsemblBacteria; ADE85166; ADE85166; RCAP_rcc01421.
DR   GeneID; 31490307; -.
DR   KEGG; rcp:RCAP_rcc01421; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_1_0_5; -.
DR   OMA; CENESWE; -.
DR   OrthoDB; 1961680at2; -.
DR   EvolutionaryTrace; P52967; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
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   Pfam; PF00258; Flavodoxin_1; 1.
DR   PIRSF; PIRSF038996; FldA; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Flavoprotein; FMN; Nitrogen fixation;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..182
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171641"
FT   DOMAIN          4..173
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   CONFLICT        124..125
FT                   /note="KL -> NV (in Ref. 1; AAC05792)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           14..23
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           110..119
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           161..171
FT                   /evidence="ECO:0007829|PDB:2WC1"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:2WC1"
SQ   SEQUENCE   182 AA;  19848 MW;  955F326BBF27213E CRC64;
     MAKIGLFFGS DTGTTRKIAK QIKDMFDDEV MAKPLNVNRA DVADFMAYDF LILGTPTLGD
     GQLPGLSANA ASESWEEFLP RIADQDFSGK TIALFGLGDQ VTYPLEFVNA LFFLHEFFSD
     RGAKLVGRWP AKGYGFEDSL AVVEGEFLGL ALDQDNQAAL TPERLKGWLS LIAADFGLVL
     PA