FPRA_RHOCA
ID FPRA_RHOCA Reviewed; 435 AA.
AC P0CY93; P18607; Q52692; Q52717;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Type A flavoprotein fprA;
DE EC=1.-.-.-;
DE AltName: Full=FMN protein fprA;
DE AltName: Full=Flavoprotein A;
GN Name=fprA;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10S;
RX PubMed=8264535; DOI=10.1007/bf00279903;
RA Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA Schuppler M., Marxer M., Oelze J., Klipp W.;
RT "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT capsulatus: a putative membrane complex involved in electron transport to
RT nitrogenase.";
RL Mol. Gen. Genet. 241:602-615(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-435.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=2402451; DOI=10.1093/nar/18.17.5284;
RA Jouanneau Y., Richaud P., Grabau C.;
RT "The nucleotide sequence of a flavodoxin-like gene which precedes two
RT ferredoxin genes in Rhodobacter capsulatus.";
RL Nucleic Acids Res. 18:5284-5284(1990).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9660187; DOI=10.1046/j.1432-1327.1998.2540325.x;
RA Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.;
RT "A family of flavoproteins in the domains Archaea and Bacteria.";
RL Eur. J. Biochem. 254:325-332(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51402.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB37851.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X72888; CAA51402.1; ALT_INIT; Genomic_DNA.
DR EMBL; X54054; CAB37851.1; ALT_INIT; Genomic_DNA.
DR PIR; S39896; S39896.
DR AlphaFoldDB; P0CY93; -.
DR SMR; P0CY93; -.
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; 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; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Electron transport; Flavoprotein; FMN; Iron; Metal-binding; Oxidoreductase;
KW Transport.
FT CHAIN 1..435
FT /note="Type A flavoprotein fprA"
FT /id="PRO_0000216806"
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 VARIANT 265
FT /note="W -> R (in strain: ATCC 33303 / B10)"
FT VARIANT 285
FT /note="R -> A (in strain: ATCC 33303 / B10)"
FT VARIANT 289..290
FT /note="QL -> HV (in strain: ATCC 33303 / B10)"
FT VARIANT 423
FT /note="R -> A (in strain: ATCC 33303 / B10)"
SQ SEQUENCE 435 AA; 48103 MW; 09BFC53D8BEF7EB6 CRC64;
MSVPPFTIRP AAPRLDGPTG PVAVAPGVHW VGALDPGLRN FDVILKTANG TTYNAYAVRG
SEGVAVIDTV KAEFAGDFFA RLEAVARYDE IRLIVLNHLE PDHTGAVPEL LRRAPQAQVR
LSPRGLPMLR ALLKDDFERY DIKGVTTGQS VSLGDRICSF FTTPFVHWPD TQCTWLAAER
VLFTCDLFGS HYCDGRLFND LVGDFRFSFE YYFDRIMRPF RSFVAQVLDL IEPLDFGIIA
PAHGPILRSH PRDYLTHTRR LISSWLAAET GSEKTLLIFY VSAYRATAQL AQAIHDGAAE
SPDVRVSLFD LEGGEITPFL DLIEEADGIA LGTPTINGDA VRTIWEMLAA LVDIETRGKL
GAAFGSYGWS GEAVRLVETR LQGLKMRLPE PGLRVKLHPS AAELEEGRAF GRRLADHLTG
RARPREVDFA EIAAR
