Sulfite reductase, dissimilatory-type subunit alpha - Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)

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Reviewed, UniProtKB/Swiss-Prot P45574 (DSVA_DESVH)

Last modified June 16, 2009. Version 61. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Sulfite reductase, dissimilatory-type subunit alpha
    EC=1.8.99.3
Alternative name(s):
    Desulfoviridin subunit alpha
    Hydrogensulfite reductase subunit alpha

Gene names

Name:	dsvA
Ordered Locus Names:	DVU_0402

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Complete proteome] [HAMAP]

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

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Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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. Binds 2 sirohemes per subunit.
Subunit structure	Heterohexamer of two alpha, two beta and two gamma subunits.
Sequence similarities	Contains 1 4Fe-4S ferredoxin-type domain.

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Ontologies

Keywords
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro hydrogensulfite reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 437

436

Sulfite reductase, dissimilatory-type subunit alpha

PRO_0000080030

Regions

Domain

294 – 322

4Fe-4S ferredoxin-type

Sites

Metal binding

177

Iron (heme axial ligand) Potential

Metal binding

183

Iron (heme axial ligand) Potential

Metal binding

221

Iron (heme axial ligand) Potential

Metal binding

225

Iron (heme axial ligand) Potential

Metal binding

284

Iron-sulfur (4Fe-4S) Potential

Metal binding

303

Iron-sulfur (4Fe-4S) Potential

Metal binding

306

Iron-sulfur (4Fe-4S) Potential

Metal binding

309

Iron-sulfur (4Fe-4S) Potential

Experimental info

Sequence conflict

S → V AA sequence Ref.3

Sequence conflict

Q → K AA sequence Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P45574-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4AED624D4B13A21F
Show »

FASTA

437

49,091

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR." Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G. Appl. Environ. Microbiol. 61:290-296(1995) [PubMed: 7887608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." 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. Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The third subunit of desulfoviridin-type dissimilatory sulfite reductases." Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G., Hagen W.R. Eur. J. Biochem. 205:111-115(1992) [PubMed: 1555572] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U16723 Genomic DNA. Translation: AAA70107.1.
AE017285 Genomic DNA. Translation: AAS94885.1.

PIR

S21197.

RefSeq

YP_009626.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V4J	X-ray	2.10	A/D	1-437	[»]

ModBase

Search...

Genome annotation databases

GeneID

2796152.

GenomeReviews

Gene locus DVU_0402 in contig AE017285_GR.

KEGG

dvu:DVU0402.

TIGR

DVU_0402.

Phylogenomic databases

HOGENOM

P45574.

OMA

P45574. DIMLQGI.

Enzyme and pathway databases

BioCyc

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

BRENDA

1.8.99.3. 3169.

Family and domain databases

InterPro

IPR017896. 4Fe4S_Fe-S-bd.
IPR011806. DsrA.
IPR006067. Nir_Sir_4Fe4S.
[Graphical view]

Pfam

PF01077. NIR_SIR. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02064. dsrA. 1 hit.

PROSITE

PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

DSVA_DESVH

Accession

Primary (citable) accession number: P45574
Secondary accession number(s): Q46581

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families