ID   E4T7I7_PALPW            Unreviewed;       604 AA.
AC   E4T7I7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   01-MAY-2013, entry version 18.
DE   SubName: Full=Sulfite reductase (NADPH) flavoprotein, alpha chain;
GN   OrderedLocusNames=Palpr_2549;
OS   Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Paludibacter.
OX   NCBI_TaxID=694427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB4;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17365 / JCM 13257 / WB4;
RX   DOI=10.4056/sigs.1503846;
RA   Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C.,
RA   Brambilla E., Rohde M., Goker M., Detter J., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.;
RT   "Complete genome sequence of Paludibacter propionicigenes type strain
RT   (WB4).";
RL   Stand. Genomic Sci. 4:36-44(2011).
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; CP002345; ADQ80681.1; -; Genomic_DNA.
DR   RefSeq; YP_004043666.1; NC_014734.1.
DR   EnsemblBacteria; ADQ80681; ADQ80681; Palpr_2549.
DR   GeneID; 10000219; -.
DR   KEGG; ppn:Palpr_2549; -.
DR   PATRIC; 45313219; VBIPalPro155528_2598.
DR   HOGENOM; HOG000282025; -.
DR   KO; K00380; -.
DR   BioCyc; PPRO694427:GHIQ-2608-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:InterPro.
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:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   Gene3D; 1.20.990.10; -; 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.
SQ   SEQUENCE   604 AA;  67628 MW;  2C8A0583F60CB21F CRC64;
     MNINTSPLSD DQIELFTRLT NSLSKEQLAW VSGYLAGFSA SGVSSESPEI QEPVAETNIQ
     NTLTILYGSR TGNGEGLAKK ALKMATEQGL NATIKSMADY KVRDLQSEKN LLVIVSTHGE
     GVPPFAAREL HEFIYSKRAP KLENTTFAVL ALGDSSYFQF CKTGKDFDEQ LEKLGAKRLV
     PRIACDVDFE EAAENWLKAT LPAFGDGKAT AKAKPQFRLD IPVKVSVAEK KPEAHTKKNP
     FMAPVYEKIS LHGKGSKRQT LHIELSTENA PGLDYEPGDA AGVYPLNSAE LVGDVLAVTG
     LNAGDFVIFN GVEKKLETAL HRNVELSKIT TDVVGRYLET YPNKKLKKLS EDTDKFKEYL
     DGRDIVDLLQ DYPSEITAEN LIKILRPLQP RYYSIASSPK AYPGELHLTV GVVNYENAGR
     EKYGTCSTYL SEVEVEDEKV PIFIERNPGF RLPENDETPI IMVGAGTGIA PYRAFVQHRE
     LAEKPGKSWL FFGNRNFETE FLYQTEWQGF LKSGALTKMD VAFSRDGDKK VYVQDRLLEN
     AKEVYQWLEE GSNFYICGDM KNMARHVQDT LVKIVEKEGV MTKENAQEYV ANLEKERRLQ
     LDVY
//