[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0005-2728(93)90037-G; PubMed=8347657 [NCBI, ExPASy, EBI, Israel, Japan] Gisselmann G., Klausmeier P., Schwenn J.D.; "The ferredoxin:sulphite reductase gene from Synechococcus PCC7942."; Biochim. Biophys. Acta 1144:102-106(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.; "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: Hydrogen sulfide + 6 oxidized ferredoxin + 3 H₂O = sulfite + 6 reduced ferredoxin + 6 H⁺.
COFACTOR: Binds 1 siroheme per subunit.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
SUBUNIT: Monomer.
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

Z11755; CAA77809.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000100; ABB56051.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_399038.1; -.

3D structure databases

HSSP

P17846; 4AOP. [HSSP ENTRY / PDB]

ModBase

P30008.

Enzyme and pathway databases

BioCyc

SELO1140:SYNPCC7942_0019-MON; -.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050311;	Molecular function: sulfite reductase (ferredoxin) activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
IPR011787; Sir.
Graphical view of domain structure.

Pfam

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

PR00397; SIROHAEM.

TIGR02042; sir; 1.

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

3774239; -.

GenomeReviews

CP000100_GR; Synpcc7942_0019.

KEGG

syf:Synpcc7942_0019; -.

Phylogenomic databases

HOGENOM

P30008; -.

Genome annotation databases

CMR

P30008; Synpcc7942_0019.

Other

UniRef

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

Keywords

4Fe-4S; Complete proteome; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Thioether bond.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 624`	`624`	`Sulfite reductase [ferredoxin].`	`PRO_0000199953`
`METAL`	`446 446`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`452 452`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`491 491`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`495 495`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`495 495`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CROSSLNK`	`52 137`		`3'-(S-cysteinyl)-tyrosine (Tyr-Cys) (By similarity).`
`CONFLICT`	`587 587`		`R -> G (in Ref. 1; CAA77809).`

Sequence information

Length: 624 AA [This is the length of the unprocessed precursor]

Molecular weight: 70131 Da [This is the MW of the unprocessed precursor]

CRC64: E5AABAFD6BBF4539 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPTAAPQKL SKVEDLKARS QYLLEPILSQ LQEESTHFNE DGIQILKFHG SYQQDNRDNR 

        70         80         90        100        110        120 
VKGQEKDFQF MLRLRSPGGY IPPQLYLTLD QLADDYGNGT LRATTRQAFQ LHGILKRDLK 

       130        140        150        160        170        180 
TVIRRIVENL GSTISACGDV NRNVMAPPAP FRDRPEYEWA RTYANNIADL LTPESGAYYE 

       190        200        210        220        230        240 
LWLDGEKVLS GEPDPAVLAA RRNPKGRVAD SVEPLYSDRY LPRKFKIAVT VPGDNSIDLF 

       250        260        270        280        290        300 
TQDIGLVVIG NDRGELEGFN VYVGGGMGRT HNKEETFARL ADPLGFVPAA DIYAAVQAIV 

       310        320        330        340        350        360 
ATQRDYGDRS NRRHARMKYL IHDWGIAKFK EAVESVFGKA IAPVRELPPF RYRDYLGWHE 

       370        380        390        400        410        420 
QGDGKWFLGL PITSGRIKDD GNWQLRSALR EIVSRWQLPL LLTGSQDVLI YDVQPGDRAA 

       430        440        450        460        470        480 
IDKLLRDRGV HTVEAIDSLQ RYAMACPALP TCGLAITESE RALPGLLVRI RRLLEEQGLP 

       490        500        510        520        530        540 
DEHFVVRMTG CPNGCARPYM AELAFVGSAP NTYQLWLGGS PDQTRLARPF IDRLADGDVE 

       550        560        570        580        590        600 
TQLRPLFVFF KQSRQAGESF GDFCDRVGFD ALRQFSESYQ HEAAKPRYRV GLRADVHGRL 

       610        620 
KAEADKRGVS LTDLACEAIA AYLR

P30008 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