(data stored in ACNUC7421 zone)

SWISSPROT: Q8X4N3_ECO57

ID   Q8X4N3_ECO57            Unreviewed;       441 AA.
AC   Q8X4N3; Q7AHA4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   08-MAY-2019, entry version 138.
DE   SubName: Full=Pyridine nucleotide-dependent disulfide oxidoreductase of reactive chlorine stress species RCS resistance {ECO:0000313|EMBL:BAB33765.2};
GN   Name=rclA {ECO:0000313|EMBL:BAB33765.2};
GN   ORFNames=ECs_0342 {ECO:0000313|EMBL:BAB33765.2};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33765.2, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33765.2, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; BA000007; BAB33765.2; -; Genomic_DNA.
DR   RefSeq; NP_308369.2; NC_002695.1.
DR   RefSeq; WP_001046339.1; NZ_SDVX01000001.1.
DR   STRING; 155864.EDL933_0344; -.
DR   EnsemblBacteria; AAG54638; AAG54638; Z0381.
DR   EnsemblBacteria; BAB33765; BAB33765; BAB33765.
DR   GeneID; 914441; -.
DR   KEGG; ecs:ECs0342; -.
DR   PATRIC; fig|386585.9.peg.435; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   KO; K21739; -.
DR   BioCyc; ECOO157:YKGC-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X4N3.
DR   SWISS-2DPAGE; Q8X4N3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
FT   NP_BIND     165    172       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    426    426       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      52     52       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     188    188       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     251    251       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     292    292       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     43     48       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   441 AA;  48239 MW;  7A992E15B6769EB8 CRC64;
     MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP TKTLVHDAQQ
     HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVINGQAE FINNHSLRVH RPEGNLEIHG
     EKIFINTGAQ TVVPPIPGIT TTPGVYDSTG LLNLKELPGH LGILGGGYIG VEFASMFANF
     GSKVTILEAA SLFLPREERD IADNIATILR DQGVDIILNA HVERISHHEN QVQVHSEHAQ
     LAVDALLIAS GRQPATASLH PENAGIAVNE RGAIVVDKRL HTTADNIWAM GDVTGGLQFT
     YISLDDYRIV RDELLGEGKR STDDRKNVPY SVFMTPPLSR VGMTEEQARE SGADIQVVTL
     PVAAIPRARV MNDTRGVLKA IVDNKTQRIL GASLLCVDSH EMINIVKMVM DAGLPYSILR
     DQIFTHPSMS ESLNDLFSLV K
//

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