ID E8XGY6_SALT4 Unreviewed; 428 AA.
AC E8XGY6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN Name=fixC {ECO:0000313|EMBL:ADX15825.1};
GN OrderedLocusNames=STM474_0081 {ECO:0000313|EMBL:ADX15825.1};
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX15825.1, ECO:0000313|Proteomes:UP000008978};
RN [1] {ECO:0000313|EMBL:ADX15825.1, ECO:0000313|Proteomes:UP000008978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX PubMed=21478351; DOI=10.1128/JB.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
CC -!- FUNCTION: Could be part of an electron transfer system required for
CC anaerobic carnitine reduction. {ECO:0000256|ARBA:ARBA00037588}.
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; CP002487; ADX15825.1; -; Genomic_DNA.
DR RefSeq; WP_001287777.1; NC_016857.1.
DR AlphaFoldDB; E8XGY6; -.
DR KEGG; seb:STM474_0081; -.
DR PATRIC; fig|909946.3.peg.85; -.
DR HOGENOM; CLU_050977_0_0_6; -.
DR Proteomes; UP000008978; 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; 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:SF1; PROTEIN FIXC; 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 7..185
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 428 AA; 45744 MW; 235A007B4F710827 CRC64;
MSEDIFDAII VGAGLAGSVA ALVLAREGAQ VLVIERGNSA GAKNVTGGRL YAHSLERIIP
GFADQAPIER MITHEKLAFM TDNGAMTIDY CNGEDASASQ VSYSVLRSKF DAWLMEQAEE
AGAQLITGIR VDNVVQRDGK VVGVEADGDI LEAKVVILAD GVNSLLAEKL GMTKRVEASH
VAVGVKELIE LPKSVIEDRF QLQGNEGAAC LFAGAPTDGL MGGGFLYTNE TTLSLGLVCG
LHHLKDAKKS VPQMLEDFKQ HPAVAPLIAG GKLVEYAAHV VPEAGMNMQP ELVGDGVLIA
GDAAGMCMNL GFTIRGMDLA ISAGEAAAKT VLSAMKRDDF SKQSLGEYRQ HLDEGPMRDM
RMYQKLPAFL DNPRMFTAYP EMAVNIARDL FTVDGSAPVP MRKKILRHAK KVGFINLMKD
GLKGVTVL
//
