ID A0A0R3MXK7_9BRAD Unreviewed; 433 AA.
AC A0A0R3MXK7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN ORFNames=CQ14_35825 {ECO:0000313|EMBL:KRR24302.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR24302.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR24302.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR24302.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRR24302.1}.
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DR EMBL; LLYB01000064; KRR24302.1; -; Genomic_DNA.
DR RefSeq; WP_057858615.1; NZ_LLYB01000064.1.
DR AlphaFoldDB; A0A0R3MXK7; -.
DR OrthoDB; 9795712at2; -.
DR Proteomes; UP000051660; 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 PRINTS; PR00411; PNDRDTASEI.
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 433 AA; 48435 MW; FFCBB77102048950 CRC64;
MIEERFDAIV VGAGMAGNAA ALTMAKRGMK VLQLERGEYS GSKNVRAAIL DGDIMEQLAP
DFREGAPLER RLVEQRFWLL DSRSHVGLRY RFNDCNTKRP NQYIVIRALF DKWFSRKVRE
AGATVLYQST VTELAQNCRG RVIGVRTDRQ DGIIHADVVV LAEGANGWLG TRAGLRERLT
PDQIALQVKE MHLLPREIIE SRFNLKRDEG VIIEAAGTIS RGMTGMGFIY ANRECISLGI
GCLVSDLQRT GETPYGLLER FKRHPSILPL INGSELKEYS AHLIPKRGYN TIPQLYGKGW
VVVGDAAELN NTSDCGRLNL AIISGRIAAE AIFRVKSRGA RSTSSTLSLY KKMLNESYED
LKNDKYMPAL IHTQPENFLL SYPQLVSKAI VNFARFGVGP KAGEGKPNSK CFCDMWSWTG
LFGDGFRLPR AWR
//
