[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3888621 [NCBI, ExPASy, EBI, Israel, Japan] Voordouw G., Brenner S.; "Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough)."; Eur. J. Biochem. 148:515-520(1985).
[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 35-69. DOI=10.1016/0006-291X(87)90376-7; PubMed=3322275 [NCBI, ExPASy, EBI, Israel, Japan] Prickril B.C., He S.H., Li C., Menon N.K., Choi E.S., Przybyla A.E., Dervartanian D.V., Peck H.D. Jr., Fauque G., le Gall J., Teixeira M., Moura I., Moura J.J.G., Patil D., Huynh B.H.; "Identification of three classes of hydrogenase in the genus, Desulfovibrio."; Biochem. Biophys. Res. Commun. 149:369-377(1987).
[4]	SIGNAL SEQUENCE CLEAVAGE SITE. PubMed=3525521 [NCBI, ExPASy, EBI, Israel, Japan] Prickril B.C., Czechowski M.H., Przybyla A.E., Peck H.D. Jr., le Gall J.; "Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris."; J. Bacteriol. 167:722-725(1986).
[5]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). DOI=10.1016/S0969-2126(99)80005-7; PubMed=10368269 [NCBI, ExPASy, EBI, Israel, Japan] Nicolet Y., Piras C., Legrand P., Hatchikian E.C., Fontecilla-Camps J.-C.; "Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center."; Structure 7:13-23(1999).

Comments

FUNCTION: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
CATALYTIC ACTIVITY: H₂ + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H⁺.
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

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

X02416; CAA26267.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017285; AAS96247.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B24551; HQDVFS.

RefSeq

YP_010988.1; -.

3D structure databases

PDB

1E08; NMR; -; D=36-123.	[ExPASy / RCSB / EBI]
1GX7; NMR; -; D=36-123.	[ExPASy / RCSB / EBI]
1HFE; X-ray; 1.60 A; S/T=1-123.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1E08; -.
1GX7; -.
1HFE; -.

ModBase

P07603.

Protein-protein interaction databases

DIP

DIP:6187N; -.

Enzyme and pathway databases

BioCyc

DVUL882:DVU_1770-MON; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0051536;	Molecular function: iron-sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003149; Fe_hydrogenase_ssu-like.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.260.20; Fe_hyd_ssu-like; 1.

Pfam

PF02256; Fe_hyd_SSU; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01409; TAT_signal_seq; 1.

PROSITE

PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

2795817; -.

GenomeReviews

AE017285_GR; DVU_1770.

KEGG

dvu:DVU1770; -.

TIGR

DVU_1770; -.

Phylogenomic databases

HOGENOM

P07603; -.

Other

P07603; -.

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

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 34`	`34`	`Tat-type signal.`
`CHAIN`	`35 123`	`89`	`Periplasmic [Fe] hydrogenase small subunit.`	`PRO_0000013413`
`HELIX`	`39 56`	`18`
`HELIX`	`62 64`	`3`
`HELIX`	`66 74`	`9`
`HELIX`	`82 88`	`7`
`HELIX`	`97 104`	`8`
`HELIX`	`113 116`	`4`

Sequence information

Length: 123 AA [This is the length of the unprocessed precursor]

Molecular weight: 13624 Da [This is the MW of the unprocessed precursor]

CRC64: 2F4F7A4304ECD47B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQIASITRRG FLKVACVTTG AALIGIRMTG KAVAAVKQIK DYMLDRINGV YGADAKFPVR 

        70         80         90        100        110        120 
ASQDNTQVKA LYKSYLEKPL GHKSHDLLHT HWFDKSKGVK ELTTAGKLPN PRASEFEGPY 


PYE

P07603 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