[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 219 / 6311; PubMed=8695637 [NCBI, ExPASy, EBI, Israel, Japan] Bruehl A., Haverkamp T., Gisselmann G., Schwenn J.D.; "A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase."; Biochim. Biophys. Acta 1295:119-124(1996).

Comments

FUNCTION: This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (By similarity).
CATALYTIC ACTIVITY: H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH.
COFACTOR: Binds 1 siroheme per subunit (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z23169; CAA80688.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S34191; S34191.

3D structure databases

HSSP

P17846; 7GEP. [HSSP ENTRY / PDB]

ModBase

P52673.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019344;	Biological process: cysteine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011786; CysI.
IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
Graphical view of domain structure.

Pfam

PF01077; NIR_SIR; 1.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.

PR00397; SIROHAEM.

TIGR02041; CysI; 1.

PS00365; NIR_SIR; 1.

Other

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

Keywords

4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 559`	`559`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_0000199911`
`METAL`	`423 423`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`429 429`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`468 468`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`472 472`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`472 472`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 559 AA [This is the length of the unprocessed precursor]

Molecular weight: 62272 Da [This is the MW of the unprocessed precursor]

CRC64: 6337D0DE9C941C70 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAPIHENER IKARSNCLRG TLRESLADTL TGAISPEDTQ ISKFHGFYQQ DHRDRRQARP 

        70         80         90        100        110        120 
EQYLEPYFGF MLRAPLPGGV CTPAQWLAID GMGRELGGGS LRLTTRQSFQ YHGILKRDIA 

       130        140        150        160        170        180 
SVIRGINAVM IDSIGGCGDV NRNVLCNPNP VESALHREVY DWAKRISEHL LPRTRAYHEI 

       190        200        210        220        230        240 
WLDGEQVGGG EDVEPIYGRT YLPRKFKTAV GVPPHNDVDV YANDLGFAAV ADGSRLIGFN 

       250        260        270        280        290        300 
VSAGGTGRNT GIPATFPRLA DVLGFVEPER TLAVAEAVVT TQRHFGDRLD RTQARLKYTI 

       310        320        330        340        350        360 
ERMGLDAFRD EVERRAGIRF APARPIGFTD QGDRTAWVRG QDGRWHLTLY IESGRLIDGP 

       370        380        390        400        410        420 
GQSSMQGLRE IARIHQGDFR ITPNQNLIVA RVPEPGKSEI EALARKYGLL DKGIALRLNG 

       430        440        450        460        470        480 
MSCVALPTCP LAMAEAERYY PDFLAQVERL TRKHGLAEQE IVTRMTGCPN GCARPYLAEL 

       490        500        510        520        530        540 
ALVGKGPGRY NLMLGGNGRR YRLNRLYREN LDEAAILAEI DTLLGRYAAC RQPGERFGDY 

       550 
LIRDGIVRPV VNPAEDFHE

P52673 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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