ID D3GDJ7_RHILV Unreviewed; 435 AA.
AC D3GDJ7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387 {ECO:0000313|EMBL:ACV50407.1};
RN [1] {ECO:0000313|EMBL:ACV50407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8401 {ECO:0000313|EMBL:ACV50407.1};
RX PubMed=19727520; DOI=10.1093/abbs/gmp060;
RA Zhang Y., Hong G.;
RT "Post-transcriptional regulation of NifA expression by Hfq and RNase E
RT complex in Rhizobium leguminosarum bv. viciae.";
RL Acta Biochim. Biophys. Sin. 41:719-730(2009).
RN [2] {ECO:0000313|EMBL:ACV50407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8401 {ECO:0000313|EMBL:ACV50407.1};
RA Hong G.F.;
RL Submitted (JAN-2009) 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; FJ648550; ACV50407.1; -; Genomic_DNA.
DR AlphaFoldDB; D3GDJ7; -.
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; PF13450; NAD_binding_8; 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}.
SQ SEQUENCE 435 AA; 47351 MW; 112C33CA09237958 CRC64;
MTKGKFDPIV IGAGMSGNAA AYSMASRGLK VLQLERGEHS GSKNVQGAIL YANMLEAIIP
NFRDDAPLER HLVEQRFWLM DDSSHTGVHY RSDDFNELKP NRYTIIRAQF DKWFSSKVRD
AGGTILCETT ATKLARNLRG KVVGVHTDRE GGVILADVVV LAEGVNGLLG TRAGLRDIPR
PENVALAVKE MHFMPEEVIA ERFGLNGSEG CVIEAGGTIS RGVAGLGFLY TNKESISVGI
GCLVSGLAGG MENPYRLLDA FKRHPSIRPL LAGSEIKEYA AHLIPEGGFK AIPQLFGDGW
VVVGDAAQLN NAVHREGSNL AMTSGLMAGE AICQIKSRGG LMTKRNLSLY KGMLDKSFVT
KDLIKHKDLP SLLHTDSHNF FMTYPTLISQ AAQNFVRVDG EPKINREKAT AASFIKARSR
WGLISDAVRS AVSWR
//
