NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1010; PubMed=15378067 [NCBI, ExPASy, EBI, Israel, Japan]
Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.;
"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens.";
Nat. Biotechnol. 22:1275-1281(2004).

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

AE016827; AAU37856.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_088441.1; -.

3D structure databases

ModBase

Q65T54.

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

3075538; -.

AE016827_GR; MS1249.

msu:MS1249; -.

fig|221988.1.peg.1170; -.

Phylogenomic databases

HOGENOM

Q65T54; -.

Genome annotation databases

CMR

Q65T54; MS1249.

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`	`1 588`	`588`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_0000199900`
`METAL`	`443 443`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`449 449`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`488 488`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`492 492`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`492 492`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 588 AA [This is the length of the unprocessed precursor]

Molecular weight: 67221 Da [This is the MW of the unprocessed precursor]

CRC64: C687B9D48C5C0399 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDKKQKGLE WQDNPLSDNE RLKEESNHLR GTILDDLEDG LTGGFKGDNF QLIRFHGMYE 

        70         80         90        100        110        120 
QDDRDIRAER QEEKLEPRKF MLLRCRLPGG IIKPEQWIEI DKFARDNNYY QSIRLTNRQT 

       130        140        150        160        170        180 
FQYHGVPKTK LQDMHRLLHK LGLDSIATAS DMNRNVLCSS NPVESELHQE AYEWAKKISE 

       190        200        210        220        230        240 
HLLPRTNGYL DVWISGKKVQ SSDSFLGQED EPILGNRYLP RKYKTAVVLP PLNDVDLYSN 

       250        260        270        280        290        300 
DMNFVGIKDE KTGKLAGFNV LVGGGLSFEH GNTKTYPNIA LELGYVPVED TLKAAESIVT 

       310        320        330        340        350        360 
TQRDFGNRAD RKNARLRYTI QNMTLEGFRE EVERRMGRRF EAIRPFEFTE RGDRIGWVKG 

       370        380        390        400        410        420 
IDKKWHLTCF IESGRLVDKP DLPLMTGMLE LAKVHKGDFR ITANQNIIIA NVAEEDKRQI 

       430        440        450        460        470        480 
EDIARQYGLI RKITKLRENA MSCVSFPTCP LAMAESERVL PEFIDELDKI MAKHHVEQDY 

       490        500        510        520        530        540 
IVTRITGCPN GCGRAMLAEI GLVGKAVGRY NLHLGGNIAG TRIPRLYKEN ITLDEILSEL 

       550        560        570        580 
DGLIARWATE RDQGEGFGDF VLRVGIIKPV VNPVVDFWDE NLIPTVAV

Q65T54 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