(data stored in SCRATCH zone)

SWISSPROT: Q3IFM2_PSEHT

ID   Q3IFM2_PSEHT            Unreviewed;       604 AA.
AC   Q3IFM2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 103.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00039990};
DE            Short=SiR-FP {ECO:0000256|PIRNR:PIRNR000207};
DE            EC=1.8.1.2 {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040368};
GN   Name=cysJ {ECO:0000313|EMBL:CAI85258.1};
GN   OrderedLocusNames=PSHAa0154 {ECO:0000313|EMBL:CAI85258.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85258.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85258.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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:0000256|PIRNR:PIRNR000207,
CC       ECO:0000256|SAAS:SAAS00040600}.
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH. {ECO:0000256|PIRNR:PIRNR000207,
CC       ECO:0000256|SAAS:SAAS00039937}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC       hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040667}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein.
CC       {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040604}.
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DR   EMBL; CR954246; CAI85258.1; -; Genomic_DNA.
DR   RefSeq; WP_011326873.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFM2; -.
DR   STRING; 326442.PSHAa0154; -.
DR   EnsemblBacteria; CAI85258; CAI85258; PSHAa0154.
DR   KEGG; pha:PSHAa0154; -.
DR   PATRIC; fig|326442.8.peg.148; -.
DR   eggNOG; ENOG4107EER; Bacteria.
DR   eggNOG; COG0369; LUCA.
DR   HOGENOM; HOG000282025; -.
DR   KO; K00380; -.
DR   OMA; TKMDVAF; -.
DR   OrthoDB; POG091H04ZI; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000006843; Chromosome I.
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-EC.
DR   GO; GO:0019344; P:cysteine biosynthetic process; 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; 3.40.50.360; -; 1.
DR   InterPro; IPR010199; CysJ.
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; 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   4: Predicted;
DR   PRODOM; Q3IFM2.
DR   SWISS-2DPAGE; Q3IFM2.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00039904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cysteine biosynthesis {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00040408};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00040169};
KW   FAD {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1,
KW   ECO:0000256|SAAS:SAAS00064062};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00064040};
KW   FMN {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1,
KW   ECO:0000256|SAAS:SAAS00064034};
KW   NADP {ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1,
KW   ECO:0000256|SAAS:SAAS00064031};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00064027, ECO:0000313|EMBL:CAI85258.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transport {ECO:0000256|PIRNR:PIRNR000207,
KW   ECO:0000256|SAAS:SAAS00064041}.
FT   DOMAIN       65    203       Flavodoxin-like. {ECO:0000259|PROSITE:
FT                                PS50902}.
FT   DOMAIN      239    453       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   NP_BIND      71     76       FMN. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     154    163       FMN. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     391    394       FAD. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     409    411       FAD. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     424    427       FAD. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     524    525       NADP. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   NP_BIND     530    534       NADP. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   BINDING     327    327       FAD. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   BINDING     566    566       NADP. {ECO:0000256|PIRSR:PIRSR000207-1}.
FT   BINDING     604    604       FAD. {ECO:0000256|PIRSR:PIRSR000207-1}.
SQ   SEQUENCE   604 AA;  65920 MW;  958B80F494E2C5CB CRC64;
     MLLGQLNAAA SPLSQEQVQK LQGLVAELNP IQQAWVSGYL AANANTAALG GAVGAAPSAG
     EAVALTILYG SQTGNAKGVA AKLKAQAESR GLAVKLVSMA DYKPTALKKE KFITVVVATY
     GEGEPPEDAE ALHEFLTTKK APKLDGVKVA VIGLGDSSYE FFCQTAKDFE QRLNTLGAET
     IYQRADLDVD YEDEATTWIT GALDAFEPDL KAQQGSSGGQ VIAMPFAGST TVASQYTKQN
     PFAAELGLVQ KITGRDSTKD VRHVEISLEG SDISYIPGDS LGVYFLNDEA RVDELLTHTQ
     IDAASLVKVA DEQLSIRDAL IEKLELTQSY PGFVEKYAIA TGTPQLLKLV EDKAAMHQYI
     EPRQIFDVVA QNPAKLDAQT LVDCLRKLQA RLYSIASSQS EVEDEVHLTV ALVEFDAFGR
     EHLGGCSGYL ARRAEEGCKV KVFSEHNDNF RLPTNDETPI IMVGPGTGIA PFRAFLQERD
     ARGASGKNWL FFGNPHFTQD FLYQVEIQGY LKSGLLSKVD VAFSRDQAEK VYVQDKLRSN
     SKAIFEWLEA GAHFYVCGDA NNMAKDVHQT LLEIIKENTG KSDEDAQQYL KDLRSANRYQ
     KDVY
//

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