FPRA_RHOCB
ID FPRA_RHOCB Reviewed; 435 AA.
AC D5ARY8; P18607; Q52692; Q52717;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Type A flavoprotein fprA;
DE EC=1.-.-.-;
DE AltName: Full=FMN protein fprA;
DE AltName: Full=Flavoprotein A;
GN Name=fprA; Synonyms=norV; OrderedLocusNames=RCAP_rcc03286;
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=8199774;
RA Saeki K., Tokuda K., Fujiwara T., Matsubara H.;
RT "Nucleotide sequence and genetic analysis of the region essential for
RT functional expression of the gene for ferredoxin I, fdxN, in Rhodobacter
RT capsulatus: sharing of one upstream activator sequence in opposite
RT directions by two operons related to nitrogen fixation.";
RL Plant Cell Physiol. 34:185-199(1993).
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 {ECO:0000305}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Note=Binds 1 FMN per monomer.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
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DR EMBL; D13625; BAA02789.2; -; Genomic_DNA.
DR EMBL; CP001312; ADE87010.1; -; Genomic_DNA.
DR RefSeq; WP_013068982.1; NC_014034.1.
DR AlphaFoldDB; D5ARY8; -.
DR SMR; D5ARY8; -.
DR STRING; 272942.RCAP_rcc03286; -.
DR EnsemblBacteria; ADE87010; ADE87010; RCAP_rcc03286.
DR GeneID; 31492066; -.
DR KEGG; rcp:RCAP_rcc03286; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_2_1_5; -.
DR OMA; HVKNNIH; -.
DR OrthoDB; 1149616at2; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport; Flavoprotein; FMN; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..435
FT /note="Type A flavoprotein fprA"
FT /id="PRO_0000410438"
FT DOMAIN 276..415
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 48..228
FT /note="Zinc metallo-hydrolase"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 405
FT /note="E -> K (in Ref. 1; BAA02789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47914 MW; 7C6353297B0250FD CRC64;
MSVPPFTIRP AAPRLDGPTG PVAVAPGVHW VGALDPGLRN FDVILKTANG TTYNAYAVRG
SEGVAVIDTV KAEFAGDFFA RLEAVARYDE IRLIVLNHLE PDHTGAVPEL LRRAPQAQVR
LSPRGLPMLR ALLKDDFERY DIKGVTTGQS VSLGDRDLQF FTTPFVHWPD TQCTWLAAER
VLFTCDLFGS HYCDGRLFND LVGDFRFSFE YYFDRIMRPF RSFVAQALDL IEPLDFGIIA
PAHGPILRSH PRDYLTHTRR LISSRLAAET GSEKTLLIFY VSAYGATAQL AQAIHDGAAE
SPDVRVSLFD LEGGEITPFL DLIEEADGIA LGTPTINGDA VRTIWEMLAA LVDIETRGKL
GAAFGSYGWS GEAVRLVETR LQGLKMRLPE PGLRVKLHPS AAELEEGRAF GRRLADHLTG
RAAPREVDFA EIAAR
