Reviewed, UniProtKB/Swiss-Prot Q06173 (PHNS1_DESVH)

Names and origin

Protein names

Recommended name:
    Periplasmic [NiFe] hydrogenase small subunit 1
    EC=1.12.2.1
Alternative name(s):
    NiFe hydrogenlyase small chain 1

Gene names

Name:	hynB1
Synonyms:	hynB-1
Ordered Locus Names:	DVU_1921

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	317 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)

Catalytic activity	2 H2 + ferricytochrome c3 = 4 H+ + ferrocytochrome c3.
Cofactor	Binds 1 3Fe-4S cluster By similarity. Binds 2 4Fe-4S clusters By similarity.
Subunit structure	Heterodimer of a large and a small subunit.
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ferredoxin hydrogenase complex Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro cytochrome-c3 hydrogenase activity Inferred from electronic annotation. Source: EC ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 49	49	Tat-type signal Potential
	Chain	50 – 317	268	Periplasmic [NiFe] hydrogenase small subunit 1		PRO_0000013417
Sites
	Metal binding	67	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	70	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	164	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	200	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	238	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	241	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	266	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	272	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	281	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	299	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	302	1	Iron-sulfur 3 (3Fe-4S) By similarity
Experimental info
	Mutagenesis	18	1	R → E: Completely inhibits export and processing of the fusion protein. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q06173-1 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: E579C0215F1C5F47	FASTA	317	34,236
	10 20 30 40 50 60 MRFSVGLGKE GAEERLARRG VSRRDFLKFC TAIAVTMGMG PAFAPEVARA LTGSRRPSVV 70 80 90 100 110 120 YLHNAECTGC SESVLRAFQP YLDELILDTI SLDYHETIMA AAGDAAEAAL HQAVANPDGF 130 140 150 160 170 180 ICIVEGAIPT ADNGIYGKVA NHTMLSICSD IVPKAKAVIA YGTCATFGGV QAAKPNPTGA 190 200 210 220 230 240 KGLNDALKHL GVNAINLAGC PPNPYNLVGT LVYYLKNNAA PEMDEFNRPL MFFGQSVHDN 250 260 270 280 290 300 CPRLKHFDAG EFAPSFESEE ARKGWCLYEL GCKGPSTMNN CPKIKFNQTN WPVEAGHPCI 310 GCSEPDFWDE KSPFYES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein." Niviere V., Wong S.L., Voordouw G. J. Gen. Microbiol. 138:2173-2183(1992) [PubMed: 1479348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, MUTAGENESIS OF ARG-18.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017285 Genomic DNA. Translation: AAS96397.1.
RefSeq	YP_011138.1.
3D structure databases
SMR	Q06173. Positions 51-317.
ModBase	Search...
Genome annotation databases
GeneID	2793337.
GenomeReviews	Gene locus DVU_1921 in contig AE017285_GR.
KEGG	dvu:DVU1921.
TIGR	DVU_1921.
Phylogenomic databases
HOGENOM	Q06173.
OMA	Q06173. RLIHENC.
Enzyme and pathway databases
BioCyc	DVUL882:DVU_1921-MON.
Family and domain databases
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR001821. NiFe_hydrogenase_ssu. IPR006311. Tat. IPR017909. Twin_arg_translocation_Tat. [Graphical view]
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
PIRSF	PIRSF000310. NiFe_hyd_ssu. 1 hit.
PRINTS	PR00614. NIHGNASESMLL.
TIGRFAMs	TIGR00391. hydA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHNS1_DESVH

Accession

Primary (citable) accession number: Q06173

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 24, 2004
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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