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 01-MAY-2013, entry version 53.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE Short=SiR-FP;
DE EC=1.8.1.2;
GN Name=cysJ; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC NADPH.
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC the beta component is a hemoprotein (By similarity).
CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR EMBL; CP000247; ABG70727.1; -; Genomic_DNA.
DR RefSeq; YP_670628.1; 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 GeneID; 4191563; -.
DR KEGG; ecp:ECP_2738; -.
DR PATRIC; 18196302; VBIEscCol77757_2778.
DR eggNOG; COG0369; -.
DR HOGENOM; HOG000282025; -.
DR KO; K00380; -.
DR OMA; SDKDVRH; -.
DR PhylomeDB; Q0TEA2; -.
DR ProtClustDB; PRK10953; -.
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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:HAMAP.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:HAMAP.
DR GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR Gene3D; 1.20.990.10; -; 1.
DR HAMAP; MF_01541; CysJ; 1; -.
DR InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; FAD-binding_1.
DR InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR InterPro; IPR001094; Flavdoxin.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; SSF63380; Riboflavin_synthase_like_b-brl; 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; Complete proteome; Cysteine biosynthesis;
KW Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW Transport.
FT CHAIN 1 599 Sulfite reductase [NADPH] flavoprotein
FT alpha-component.
FT /FTId=PRO_0000292968.
FT DOMAIN 64 202 Flavodoxin-like.
FT DOMAIN 234 448 FAD-binding FR-type.
FT NP_BIND 70 74 FMN (By similarity).
FT NP_BIND 117 122 FMN (By similarity).
FT NP_BIND 150 181 FMN (By similarity).
FT NP_BIND 386 389 FAD (By similarity).
FT NP_BIND 420 422 FAD (By similarity).
FT NP_BIND 519 527 NADP (By similarity).
FT BINDING 489 489 NADP (By similarity).
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
//
