(data stored in SCRATCH zone)

SWISSPROT: C8U1Z5_ECO10

ID   C8U1Z5_ECO10            Unreviewed;       441 AA.
AC   C8U1Z5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=Predicted oxidoreductase {ECO:0000313|EMBL:BAI29153.1};
GN   Name=ykgC {ECO:0000313|EMBL:BAI29153.1};
GN   OrderedLocusNames=ECO103_0280 {ECO:0000313|EMBL:BAI29153.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29153.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29153.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010958; BAI29153.1; -; Genomic_DNA.
DR   RefSeq; WP_001046313.1; NC_013353.1.
DR   EnsemblBacteria; BAI29153; BAI29153; ECO103_0280.
DR   KEGG; eoh:ECO103_0280; -.
DR   HOGENOM; HOG000276709; -.
DR   KO; K21739; -.
DR   OMA; VHIIHHN; -.
DR   BioCyc; ECOL585395:ECO103_RS01470-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U1Z5.
DR   SWISS-2DPAGE; C8U1Z5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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}.
FT   DOMAIN        5    296       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      328    434       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
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;  48184 MW;  3ABA634D1006E93E CRC64;
     MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP TKTLVHDAQQ
     HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVIDGQAE FINNHSLRVH RPEGNLEIHG
     EKIFINTGAQ TVVPPIPGIT TTPGVYDSTG LLNLKELPGH LGILGGGYIG VEFASMFANF
     GSKVTILEAA SLFLPREDRD IADNIATILR DQGVDIILNA HVERISHNEN QVQVHSEHAQ
     LAVDALLIAS GRQPATASLH PENAGIAVNE RGAIVVDKQL HTTADNIWAM GDVTGGLQFT
     YISLDDYRIV RDELLGEGRR STDDRKNVPY SVFMTPPLSR VGMTEEQARE SGADIQVVTL
     PVAAIPRARV MNDTRGVLKA IVDNKTQRIL GASLLCVDSH EMINIVKMVM DAGLPYSILH
     DQIFTHPSMS ESLNDLFSLV K
//

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