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Database: UniProt
Entry: Q0TEA2
LinkDB: Q0TEA2
Original site: Q0TEA2 
ID   CYSJ_ECOL5              Reviewed;         599 AA.
AC   Q0TEA2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   06-JUL-2016, entry version 72.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541};
DE            Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541};
DE            EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541};
GN   Name=cysJ {ECO:0000255|HAMAP-Rule:MF_01541};
GN   OrderedLocusNames=ECP_2738;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Component of the sulfite reductase complex that
CC       catalyzes the 6-electron reduction of sulfite to sulfide. This is
CC       one of several activities required for the biosynthesis of L-
CC       cysteine from sulfate. The flavoprotein component catalyzes the
CC       electron flow from NADPH -> FAD -> FMN to the hemoprotein
CC       component. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC       hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
CC   -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC       flavoprotein subunit CysJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
DR   EMBL; CP000247; ABG70727.1; -; Genomic_DNA.
DR   RefSeq; WP_000211914.1; NC_008253.1.
DR   ProteinModelPortal; Q0TEA2; -.
DR   SMR; Q0TEA2; 59-599.
DR   STRING; 362663.ECP_2738; -.
DR   PRIDE; Q0TEA2; -.
DR   EnsemblBacteria; ABG70727; ABG70727; ECP_2738.
DR   KEGG; ecp:ECP_2738; -.
DR   PATRIC; 18196302; VBIEscCol77757_2778.
DR   eggNOG; ENOG4107EER; Bacteria.
DR   eggNOG; COG0369; LUCA.
DR   HOGENOM; HOG000282025; -.
DR   KO; K00380; -.
DR   OMA; GVWYEND; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; ECOL362663:GIY5-2760-MONOMER; -.
DR   UniPathway; UPA00140; UER00207.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_01541; CysJ; 1.
DR   InterPro; IPR010199; CysJ.
DR   InterPro; IPR029758; CysJ_Proteobact.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_dom.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   TIGRFAMs; TIGR01931; cysJ; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Electron transport;
KW   FAD; Flavoprotein; FMN; NADP; Oxidoreductase; Transport.
FT   CHAIN         1    599       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_0000292968.
FT   DOMAIN       64    202       Flavodoxin-like. {ECO:0000255|HAMAP-
FT                                Rule:MF_01541}.
FT   DOMAIN      234    448       FAD-binding FR-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_01541}.
FT   NP_BIND      70     75       FMN. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     117    120       FMN. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     153    162       FMN. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     386    389       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     404    406       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     419    422       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     519    520       NADP. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   NP_BIND     525    529       NADP. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   BINDING     322    322       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   BINDING     356    356       FAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   BINDING     410    410       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   BINDING     561    561       NADP. {ECO:0000255|HAMAP-Rule:MF_01541}.
FT   BINDING     599    599       FAD. {ECO:0000255|HAMAP-Rule:MF_01541}.
SQ   SEQUENCE   599 AA;  66312 MW;  9E957AD0872A050E CRC64;
     MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE
     MPGITIISAS QTGNARRVAE ALRDDLLAAK LNVKLVNAGD YKFKQIASEK LLIVVTSTQG
     EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDSSYEF FCQSGKDFDS KLAELGGERL
     LDRVDADVEY QAAASEWRAR VVDALKSRAP VAAPSQSVAT GTVNEIHTSP YSKDAPLAAS
     LSVNQKITGR NSEKDVRHIE IDLGDSGLRY QPGDALGVWY QNDPALVKEL VELLWLKGDE
     PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK LQHYAATTPI
     VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQAEVENE VHVTVGVVRY DVEGRARAGG
     ASSFLADRVE EEGEVRVFIE HNDNFRLPTN PETPVIMIGP GTGIAPFRAF MQQRAADEAP
     GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LTRIDLAWSR DQKEKIYVQD KLREQGAELW
     RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY
//
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