(data stored in ACNUC7421 zone)

SWISSPROT: B7UJF7_ECO27

ID   B7UJF7_ECO27            Unreviewed;       441 AA.
AC   B7UJF7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   SubName: Full=Predicted oxidoreductase with FAD/NAD(P)-binding domain and dimerization domain {ECO:0000313|EMBL:CAS07814.1};
GN   Name=ykgC {ECO:0000313|EMBL:CAS07814.1};
GN   OrderedLocusNames=E2348C_0266 {ECO:0000313|EMBL:CAS07814.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07814.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07814.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07814.1; -; Genomic_DNA.
DR   RefSeq; WP_001046290.1; NC_011601.1.
DR   EnsemblBacteria; CAS07814; CAS07814; E2348C_0266.
DR   KEGG; ecg:E2348C_0266; -.
DR   HOGENOM; HOG000276709; -.
DR   KO; K21739; -.
DR   OMA; VHIIHHN; -.
DR   BioCyc; ECOL574521:E2348C_RS01400-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJF7.
DR   SWISS-2DPAGE; B7UJF7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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;  48207 MW;  7A501A567CD31606 CRC64;
     MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP TKTLVHDAQQ
     HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVIDGLAE FINNHSLRVH RPGRNLEIHG
     EKIFINTGAQ AVVPPIPGIT TTPGVYDSTG LLNLKELPGH LGILGGGYIG VEFASMFANF
     GSKVTILEAA SLFLPREDRD IADNIATILR DQGVDIILNA HVERISHHEN QVQVHSEHAQ
     LAVDALLIAS GRQPATASLH PENAGIAVNE RGAIVVDKQL HTTANNIWAM GDVTGGLQFT
     YISLDDYRIV RDELLGEGRR STDDRKNVPY SVFMTPPLSR VGMTEEQARE SGADIQVVTL
     PVAAIPRARV MNDTRGVLKA IVDNKTQRIL GASLLCVDSH EMINIVKMVM DAGLPYSILR
     DQIFTHPSMS ESLNDLFSLV K
//

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