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Database: UniProt
Entry: B3Q2S2_RHIE6
LinkDB: B3Q2S2_RHIE6
Original site: B3Q2S2_RHIE6 
ID   B3Q2S2_RHIE6            Unreviewed;       435 AA.
AC   B3Q2S2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN   Name=fixC {ECO:0000313|EMBL:ACE93978.1};
GN   OrderedLocusNames=RHECIAT_PB0000270 {ECO:0000313|EMBL:ACE93978.1};
OS   Rhizobium etli (strain CIAT 652).
OG   Plasmid pB {ECO:0000313|EMBL:ACE93978.1,
OG   ECO:0000313|Proteomes:UP000008817}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE93978.1, ECO:0000313|Proteomes:UP000008817};
RN   [1] {ECO:0000313|EMBL:ACE93978.1, ECO:0000313|Proteomes:UP000008817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE93978.1,
RC   ECO:0000313|Proteomes:UP000008817};
RC   PLASMID=Plasmid pB {ECO:0000313|Proteomes:UP000008817};
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could be required for the formation of a functional
CC       nitrogenase Fe protein. Probably accepts electrons from FixA/FixB and
CC       reduces a quinone. {ECO:0000256|ARBA:ARBA00003676}.
CC   -!- FUNCTION: Part of an electron transfer system.
CC       {ECO:0000256|RuleBase:RU366069}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU366069};
CC   -!- SIMILARITY: Belongs to the ETF-QO/FixC family.
CC       {ECO:0000256|ARBA:ARBA00006796, ECO:0000256|RuleBase:RU366069}.
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DR   EMBL; CP001076; ACE93978.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3Q2S2; -.
DR   KEGG; rec:RHECIAT_PB0000270; -.
DR   HOGENOM; CLU_050977_0_0_5; -.
DR   Proteomes; UP000008817; Plasmid pB.
DR   GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR039651; FixC-like.
DR   PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR   PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU366069};
KW   Flavoprotein {ECO:0000256|RuleBase:RU366069};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366069,
KW   ECO:0000313|EMBL:ACE93978.1}; Plasmid {ECO:0000313|EMBL:ACE93978.1}.
SQ   SEQUENCE   435 AA;  48374 MW;  ABD7F0EF4F67ABEE CRC64;
     MTEENFDAIV IGAGMAGNAA AYTMSNRGMK VLQLERGEYP GSKNVQGAIM YADMLEKILP
     DFRDDAPLER HLVEQRFWMM DDSSHIGMQY RSDDFNESRH NRYTVIRAQF DKWFSRKVRE
     AGATLLCETT VTELVRDPKG KVIGVRTDRA GDVILADVVV LAEGVNGLLG TRAGLRDTPK
     PETVALAVKE MHFLAEEVID QRFGLQANEG CVIEAVGTIS RNMAGLAFLY TNKESISIGI
     GCLVSEFAAT MESPYDLLEK FKSHPSVKPL IAGAEVKEYA AHLIPEGGYK AIPQLFGDGW
     VVVGDAAQLN NAVHREGSNL AMTSGRIAGE AIVQIKNRKK PMVKENLSLY KSMLEKSFVI
     KDLRKYKDMP ALLHTNSRNF FTTYPRLLSQ AAQNFVRVDG TPKIDKERAT TGTFIKARSR
     WGLFGDAVRL ARAWR
//
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