[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7887608 [NCBI, ExPASy, EBI, Israel, Japan] Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.; "Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR."; Appl. Environ. Microbiol. 61:290-296(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nbt959; PubMed=15077118 [NCBI, ExPASy, EBI, Israel, Japan] Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; "The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough."; Nat. Biotechnol. 22:554-559(2004).
[3]	PROTEIN SEQUENCE OF 2-26. PubMed=1555572 [NCBI, ExPASy, EBI, Israel, Japan] Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G., Hagen W.R.; "The third subunit of desulfoviridin-type dissimilatory sulfite reductases."; Eur. J. Biochem. 205:111-115(1992).

Comments

FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria.
CATALYTIC ACTIVITY: (O₃S.S.SO₃)^2- + acceptor + 2 H₂O + OH^- = 3 HSO₃^- + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
COFACTOR: Binds 2 sirohemes per subunit.
SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

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

U16723; AAA70107.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017285; AAS94885.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S21197; S21197.

RefSeq

YP_009626.1; -.

3D structure databases

ModBase

P45574.

Enzyme and pathway databases

BioCyc

DVUL882:DVU_0402-MON; -.
MetaCyc:MON-12511; -.

Family and domain databases

InterPro

IPR011806; DsrA.
IPR006067; Nir_Sir_4Fe4S.
Graphical view of domain structure.

Pfam

PF01077; NIR_SIR; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02064; dsrA; 1.

PROSITE

PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P45574.

Genome annotation databases

GeneID

2796152; -.

GenomeReviews

AE017285_GR; DVU_0402.

KEGG

dvu:DVU0402; -.

TIGR

DVU_0402; -.

Phylogenomic databases

HOGENOM

P45574; -.

Other

ProtoNet

P45574.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Direct protein sequencing; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 437`	`436`	`Sulfite reductase, dissimilatory-type subunit alpha.`	`PRO_0000080030`
`DOMAIN`	`294 322`	`29`	`4Fe-4S ferredoxin-type.`
`METAL`	`177 177`		`Iron (heme axial ligand) (Potential).`
`METAL`	`183 183`		`Iron (heme axial ligand) (Potential).`
`METAL`	`221 221`		`Iron (heme axial ligand) (Potential).`
`METAL`	`225 225`		`Iron (heme axial ligand) (Potential).`
`METAL`	`284 284`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`303 303`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`306 306`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`309 309`		`Iron-sulfur (4Fe-4S) (Potential).`
`CONFLICT`	`22 22`		`S -> V (in Ref. 3; AA sequence).`
`CONFLICT`	`26 26`		`Q -> K (in Ref. 3; AA sequence).`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 49091 Da [This is the MW of the unprocessed precursor]

CRC64: 4AED624D4B13A21F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKHATPKLD QLESGPWPSF VSDIKQEAAY RAANPKGLDY QVPVDCPEDL LGVLELSYDE 

        70         80         90        100        110        120 
GETHWKHGGI VGVFGYGGGV IGRYCDQPEK FPGVAHFHTV RVAQPSGKYY SADYLRQLCD 

       130        140        150        160        170        180 
IWDLRGSGLT NMHGSTGDIV LLGTQTPQLE EIFFELTHNL NTDLGGSGSN LRTPESCLGK 

       190        200        210        220        230        240 
SRCEFACYDS QAACYELTME YQDELHRPAF PYKFKFKFDA CPNGCVASIA RSDFSVIGTW 

       250        260        270        280        290        300 
KDDIKIDAEA VKAYVAGEFK PNAGAHSGRD WGKFDIEAEV VNRCPSKCMK WDGSKLSIDN 

       310        320        330        340        350        360 
KECVRCMHCI NTMPRALHIG DERGASILCG AKAPILDGAQ MGSLLVPFVA AEEPFDEIKE 

       370        380        390        400        410        420 
VVEKIWDWWM EEGKNRERLG ETMKRLSFQK LLEVTEIAPV PQHVKEPRTN PYIFFKEEEV 

       430 
PGGWDRDITE YRKRHLR

P45574 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