NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-37; 65-71; 82-99; 124-141; 344-355; 362-368 AND 392-413.
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=7691984 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.;
"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes.";
J. Gen. Microbiol. 139:1817-1828(1993).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).

Comments

FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.
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.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius;
SUBUNIT: Heterotetramer of two alpha and two beta subunits.
SUBCELLULAR LOCATION: Membrane. Note=Although the protein complex is found in the soluble fraction it may be membrane-associated in vivo.
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

M95624; AAB17213.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000782; AAB90812.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G69302; G69302.

RefSeq

NP_069259.1; -.

3D structure databases

ModBase

Q59109.

Enzyme and pathway databases

BioCyc

AFUL224325:AF_0423-MON; -.
MetaCyc:MON-12500; -.

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

Q59109.

Genome annotation databases

GeneID

1483639; -.

GenomeReviews

AE000782_GR; AF_0423.

KEGG

afu:AF0423; -.

NMPDR

fig|224325.1.peg.418; -.

TIGR

AF_0423; -.

Phylogenomic databases

HOGENOM

Q59109; -.

Other

ProtoNet

Q59109.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 418`	`417`	`Sulfite reductase, dissimilatory-type subunit alpha.`	`PRO_0000080025`
`DOMAIN`	`277 305`	`29`	`4Fe-4S ferredoxin-type.`
`METAL`	`176 176`		`Iron (heme axial ligand) (Potential).`
`METAL`	`182 182`		`Iron (heme axial ligand) (Potential).`
`METAL`	`220 220`		`Iron (heme axial ligand) (Potential).`
`METAL`	`224 224`		`Iron (heme axial ligand) (Potential).`
`METAL`	`267 267`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`286 286`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`289 289`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`292 292`		`Iron-sulfur (4Fe-4S) (Potential).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47525 Da [This is the MW of the unprocessed precursor]

CRC64: AC12A7BFDF27EEEF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK QLEISYKDKK 

        70         80         90        100        110        120 
THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI NQPSGWFYST KALRGLCDVW 

       130        140        150        160        170        180 
EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC FEDLGNLEIP FDIGGSGSDL RTPSACMGPA 

       190        200        210        220        230        240 
LCEFACYDTL ELCYDLTMTY QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK 

       250        260        270        280        290        300 
DDIKVDQEAV KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL 

       310        320        330        340        350        360 
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD WWDEEGKFRE 

       370        380        390        400        410 
RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK DELKPSAYTE ELKKRGMW

Q59109 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