ID A0A1M3M4S3_9PROT Unreviewed; 432 AA.
AC A0A1M3M4S3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN ORFNames=BGO92_08440 {ECO:0000313|EMBL:OJX81089.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX81089.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX81089.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX81089.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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}.
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:OJX81089.1}.
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DR EMBL; MKVK01000011; OJX81089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3M4S3; -.
DR STRING; 1895778.BGO92_08440; -.
DR Proteomes; UP000184435; 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; IPR002938; FAD-bd.
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; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
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}.
FT DOMAIN 5..190
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 432 AA; 47503 MW; 28D09CA535441BB3 CRC64;
MAEKFDAIVI GAGPAGNSAA IVLARAGLKV LQLERGEYPG SKNVQGAILY AEALEQVIPN
CRRQAPLERP IIEQRMWVLD DETYVGSNYR GVKKKDEPPT RYTVIRANVD RWMSKKATDA
GVLLICEATV LDLIKQDGKV VGVRTDRVGG DIFADVVVLA DGVNSLIATK AGLRPTIKAA
DVALAVKEMH FLPKEVIEQR FNIANDEGVV IEMFGKITKG MMGTAFLYTN RESIALGIGC
MADDFKKGGI TPYDMLDEMK KHPAIKPLIA GSEVKEYAAH LIPEGGYKAI PQVHGDGWVI
CGDSGGFVNA VHREGSNLAM TTGRLAAETI IKLKEEGKPF TAQHLAAYRA QLEASFVMKD
LKKYKEMPEI FHANPQFFTT YPELLNKAAA TMLKVDNVDK KTKQKEIAGE FVKRRSYWGM
LGDAIKLVRS FR
//
