NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00124-06; PubMed=16740952 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen.";
J. Bacteriol. 188:4453-4463(2006).

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(4). 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

CP000308; ABG14831.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_652776.1; -.

3D structure databases

SMR

Q1C3Z1; 81-571.

ModBase

Q1C3Z1.

Enzyme and pathway databases

BioCyc

YPES360102:YPA_2869-MON; -.

Ontologies

GO:0009337;	Cellular component: sulfite reductase complex (NADPH) (inferred from electronic annotation from InterPro).
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:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004783;	Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
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).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01540; -; 1.
PBIL [Tree]

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.

Genome annotation databases

GeneID

4119996; -.

GenomeReviews

CP000308_GR; YPA_2869.

KEGG

ypa:YPA_2869; -.

Phylogenomic databases

HOGENOM

Q1C3Z1; -.

Genome annotation databases

CMR

Q1C3Z1; YPA_2869.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 576`	`576`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_1000068782`
`METAL`	`435 435`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`441 441`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`480 480`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`484 484`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`484 484`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 576 AA [This is the length of the unprocessed precursor]

Molecular weight: 64076 Da [This is the MW of the unprocessed precursor]

CRC64: 28AA6EF7463B6B87 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNEKHPGPLV VSGKLSDGER MKSESNFLRG TIAEDLNNGL TGGFSGDNFL LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA EQKLEPRHAM MLRCRLPGGI ITPQQWLGID KFAADNTLYG SIRITNRQTF 

       130        140        150        160        170        180 
QFHGILKGNV KPAHQLLNEL GLDALATAND VNRNVLCTSN PVESALHQEA YEWAKKISEH 

       190        200        210        220        230        240 
LLPRTRAYAE IWLDAEKVAT TDEEPILGAT YLPRKFKTTV VIPPQNDVDL HANDLNFVAV 

       250        260        270        280        290        300 
ADKGKLIGFN VLVGGGLSIA HGDKNTYPRK ASEFGYIPLK HTLAIAEAVV TTQRDWGNRT 

       310        320        330        340        350        360 
DRKNAKTKYT LERVGVETFK AEVEKRAGVS FSAIKPYQFI GRGDRIGWVK GVDKKWHLTL 

       370        380        390        400        410        420 
FVENGRLLDY PGRSLKTGVA EIAKIHQGDF RLTANQNLIV AGVPEKDKAR IEALAREHGL 

       430        440        450        460        470        480 
MDDNVTSQRE NSMACVSFPT CPLAMAEAER FLPEFVTRVE GILQQHGLAD EHIVLRVTGC 

       490        500        510        520        530        540 
PNGCGRALLA EVGLVGKAVG RYNLHLGGNR EGTRIPRMYR ENITADEILL ITDQLVGRWA 

       550        560        570 
KERHVDEGFG DFVIRAGVIA PVIDSARDFY DVQEAM

Q1C3Z1 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