ID A0A1I7M6P7_9BRAD Unreviewed; 435 AA.
AC A0A1I7M6P7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN ORFNames=SAMN05192541_12954 {ECO:0000313|EMBL:SFV17612.1};
OS Bradyrhizobium arachidis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=858423 {ECO:0000313|EMBL:SFV17612.1, ECO:0000313|Proteomes:UP000199591};
RN [1] {ECO:0000313|EMBL:SFV17612.1, ECO:0000313|Proteomes:UP000199591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26795 {ECO:0000313|EMBL:SFV17612.1,
RC ECO:0000313|Proteomes:UP000199591};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPBQ01000029; SFV17612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7M6P7; -.
DR OrthoDB; 417034at2; -.
DR Proteomes; UP000199591; Unassembled WGS sequence.
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}.
SQ SEQUENCE 435 AA; 48462 MW; 84A71B4D265EDF8E CRC64;
MIEERFDAIV VGAGMAGNAA ALTMAKRGMK VLQLERGEYP GSKNVQGAIL YADMLEKLIP
EFREEAPLER HVIEQRFWMM DDRSHVGMHY RSDEFNEERP NRYTIIRAQF DKWFSSKVRE
AGATLLCETT VTELVRDERE RIVGVRTDRR DGEIHADVVV LAEGVNGLLG TRAGLRARPR
PDNVALAVKE MHFLPRETIE ARFNLKGDEG VVIEAAGTIS RGMTGMGFIY ANKECISLGI
GCLVADFQRT GQTPYGLLDQ FKSHPSVAPL VAGTEVKEYS AHLIPEGGYK SIPQLYGEGW
VVVGDAAQLN NAIHREGSNL AMTSGRIAAE AIGLVKSRGE PMSAANLSIY KKMLDDSFVI
KDLKKYKDLP PLMHTQSQNF FLTYPQLISK AMQNFVRVDG TPKAEKEKAT LKSFVKARSW
AGLFGDACRF ARAWR
//