[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CMCP6; Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; "Complete genome sequence of Vibrio vulnificus CMCP6."; Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.

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

AE016795; AAO09852.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_760325.1; -.

3D structure databases

HSSP

P17846; 1AOP. [HSSP ENTRY / PDB]

ModBase

Q8DCK1.

Enzyme and pathway databases

BioCyc

VVUL216895:VV1_1403-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.

PRINTS

PR00397; SIROHAEM.

TIGRFAMs

TIGR02041; CysI; 1.

PROSITE

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

1178324; -.

GenomeReviews

AE016795_GR; VV1_1403.

KEGG

vvu:VV1_1403; -.

Phylogenomic databases

HOGENOM

Q8DCK1; -.

Genome annotation databases

CMR

Q8DCK1; VV1_1403.

Other

ProtoNet

Q8DCK1.

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`	`1 578`	`578`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_0000199915`
`METAL`	`441 441`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`447 447`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`487 487`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`491 491`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`491 491`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 578 AA [This is the length of the unprocessed precursor]

Molecular weight: 64943 Da [This is the MW of the unprocessed precursor]

CRC64: 146CF39788F73AD2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTFSIENNKQ VVLGEELGKL SDNERLKTQS NFLRGTIEQD LQDRITGGFT ADNFQLIRFH 

        70         80         90        100        110        120 
GMYQQDDRDI RNERAKQKLE PLHNVMLRAR MPGGIITPKQ WLAIDKFATE HSLYGSIRLT 

       130        140        150        160        170        180 
TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTTNPVESE LHQEAYEWAK 

       190        200        210        220        230        240 
KISEHLLPKT KAYAEIWLDG EKVETTEDDE PILGKTYLPR KFKTTVVIPP QNDVDVHAND 

       250        260        270        280        290        300 
LNFVAIAEKG KLIGFNVLVG GGLAMTHGDT STYPRRADDF GYIPLEKTLD VAAAVVTTQR 

       310        320        330        340        350        360 
DWGNRSNRKN AKTKYTLDRV GTDVFKAEVE KRAGIKFEVS RPYEFTERGD RIGWVEGIDG 

       370        380        390        400        410        420 
KHHLTLFIEN GRLLDYPGKP LKTGVAEIAK IHKGDFRMTA NQNLIVAGVS KSNKAKIEKL 

       430        440        450        460        470        480 
AREHGLMDEG VSEQRKNAMA CVAFPTCPLA MAEAERFLPQ FVTDVEGILD KHGLDKEDNI 

       490        500        510        520        530        540 
ILRVTGCPNG CGRAMLAEIG LVGKAPGRYN LHLGGNRGGT RVPKMYKENI TDKQILEEID 

       550        560        570 
QLVGRWANER LPNECFGDFT VRVGIIEEVI ISKRDFYA

Q8DCK1 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