ID B7JA55_ACIF2 Unreviewed; 432 AA.
AC B7JA55;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Protein FixC {ECO:0000256|RuleBase:RU366069};
GN Name=fixC {ECO:0000313|EMBL:ACK80582.1};
GN OrderedLocusNames=AFE_1478 {ECO:0000313|EMBL:ACK80582.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK80582.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK80582.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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; CP001219; ACK80582.1; -; Genomic_DNA.
DR RefSeq; WP_012536545.1; NC_011761.1.
DR AlphaFoldDB; B7JA55; -.
DR STRING; 243159.AFE_1478; -.
DR PaxDb; 243159-AFE_1478; -.
DR GeneID; 66432467; -.
DR KEGG; afr:AFE_1478; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_050977_0_0_6; -.
DR Proteomes; UP000001362; Chromosome.
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; IPR049398; ETF-QO/FixC_UQ-bd.
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; PF21162; ETFQO_UQ-bd; 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|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366069};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366069};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366069};
KW Reference proteome {ECO:0000313|Proteomes:UP000001362}.
FT DOMAIN 5..192
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 206..281
FT /note="ETF-QO/FixC ubiquinone-binding"
FT /evidence="ECO:0000259|Pfam:PF21162"
SQ SEQUENCE 432 AA; 47298 MW; B1A64797A5E5E6C8 CRC64;
MAEKFDAIVV GAGPAGNAAA YTMAKAGLSV LQLERGETPG TKNVQGAILY ADALERIIPD
FRDDAPLERH IIEQRMWVLD EKSFIGTNYR SDAFNSDQPN RYTILRAPFD KWFSGKVKEA
GALVICETTV TELIQEGKKV IGVRTDREGG DIYADVVILA DGVNSLLAKK AGFHGELEAK
NVALAVKEIH FLPEEIVQSR FNIKGNEGVV IEIAGAVTHG MVGTAFLYTN KESITLGIGC
LLSDFKNAGI APYTLLEKLK AHPAIAPLIE GGEMKEYAAH LIPEGGYKAV PTLYGEGWMI
AGDSAGLVNA VHREGSNLAM TSGRLAAETV IALKEMKLPC TAPHLARYKT ALDDSFVMKD
LRKYKELPDI LHGNPHFFSV YPQLLNRAAH TMLMVDGQDK HSKEKTIRGS FVQQRSLWGL
VGDAYRMWRA TR
//
