Reviewed, UniProtKB/Swiss-Prot P45574 (DSVA_DESVH)

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 alpha subunit

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

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.

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	(O(3)S.S.SO(3))(2-) + acceptor + 2 H(2)O + OH(-) = 3 HSO(3)(-) + 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.

Ontologies

Keywords
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	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: InterPro 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: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 437	436	Sulfite reductase, dissimilatory-type subunit alpha		PRO_0000080030
Regions
	Domain	294 – 322	29	4Fe-4S ferredoxin-type
Sites
	Metal binding	177	1	Iron (heme axial ligand) Potential
	Metal binding	183	1	Iron (heme axial ligand) Potential
	Metal binding	221	1	Iron (heme axial ligand) Potential
	Metal binding	225	1	Iron (heme axial ligand) Potential
	Metal binding	284	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	303	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	306	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	309	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	22	1	S → V AA sequence Ref.3
	Sequence conflict	26	1	Q → K AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P45574-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4AED624D4B13A21F	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

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. , 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. 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U16723 Genomic DNA. Translation: AAA70107.1. AE017285 Genomic DNA. Translation: AAS94885.1.
PIR	S21197.
RefSeq	YP_009626.1.
3D structure databases
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.
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]
Pfam	PF01077. NIR_SIR. 1 hit. [Graphical view]
TIGRFAMs	TIGR02064. dsrA. 1 hit.
PROSITE	PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

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:	November 25, 2008
This is version 56 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)