FUNCTION: Catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (By similarity).
CATALYTIC ACTIVITY: H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
COFACTOR: Binds 1 FMN per subunit (By similarity).
SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

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Cross-references

Sequence databases

EMBL

CP000653; ABP61891.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001177942.1; -.

3D structure databases

ModBase

A4WDW1.

Ontologies

GO:0004783;	Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01541; -; 1.
PBIL [Tree]

InterPro

IPR010199; CysJ.
IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

TIGRFAMs

TIGR01931; cysJ; 1.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

A4WDW1.

Genome annotation databases

GeneID

5112941; -.

GenomeReviews

CP000653_GR; Ent638_3227.

NMPDR

fig|399742.4.peg.3073; -.

CMR

A4WDW1; Ent638_3227.

Other

ProtoNet

A4WDW1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 601`	`601`	`Sulfite reductase [NADPH] flavoprotein alpha-component.`	`PRO_1000087635`
`DOMAIN`	`64 202`	`139`	`Flavodoxin-like.`
`DOMAIN`	`236 450`	`215`	`FAD-binding FR-type.`
`NP_BIND`	`70 74`	`5`	`FMN (By similarity).`
`NP_BIND`	`150 181`	`32`	`FMN (By similarity).`
`NP_BIND`	`238 290`	`53`	`FAD (By similarity).`
`NP_BIND`	`474 601`	`128`	`NADP (By similarity).`

Sequence information

Length: 601 AA [This is the length of the unprocessed precursor]

Molecular weight: 66366 Da [This is the MW of the unprocessed precursor]

CRC64: D4C25C7138BF8496 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTQAPPSNL LPLNPEQLAR LQAATTDFSP TQLAWVSGYF WGMLNQQPGA VVNAPATAVE 

        70         80         90        100        110        120 
IPAITLISAS QTGNARRVAE ALRDDLLAAK LNVNLVNAGD YKFKQIASEK LVVVVASTQG 

       130        140        150        160        170        180 
EGEPAEEAVA LHKFLFSKKA PKLDGTAFAV FGLGDTSYEF FCQSGKDFDS KLAELGAERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAAAEWRAR IVDVLKARVP KDTPAQAANS ASGAVNEVST SPYTKEEPLV 

       250        260        270        280        290        300 
ASLSVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPALVK ELVELLWLKG 

       310        320        330        340        350        360 
TEQVNVEGKT LPLSEALQWH FELTVNTANI VENYATLTRS ETLLPLVGDK AKLQHYAATT 

       370        380        390        400        410        420 
PIVDMVRFSP AQLDAEALIG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RFDIEGRARA 

       430        440        450        460        470        480 
GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAAEE 

       490        500        510        520        530        540 
APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKQKIYV QDKLREQGAE 

       550        560        570        580        590        600 
LWAWINNGAH LYVCGDANRM AKDVEQALLE VIAEFGGMDI ETADEFLSEL RVERRYQRDV 


Y

A4WDW1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools