[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2269874 [NCBI, ExPASy, EBI, Israel, Japan] Deckers H.M., Wilson F.R., Voordouw G.; "Cloning and sequencing of a [NiFe] hydrogenase operon from Desulfovibrio vulgaris Miyazaki F."; J. Gen. Microbiol. 136:2021-2028(1990).
[2]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1016/S0969-2126(97)00313-4; PubMed=9438867 [NCBI, ExPASy, EBI, Israel, Japan] Higuchi Y., Yagi T., Yasuoka N.; "Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis."; Structure 5:1671-1680(1997).
[3]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). DOI=10.1016/S0969-2126(99)80071-9; PubMed=10378274 [NCBI, ExPASy, EBI, Israel, Japan] Higuchi Y., Ogata H., Miki K., Yasuoka N., Yagi T.; "Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution."; Structure 7:549-556(1999).

Comments

FUNCTION: Catalyzes the reversible oxidoreduction of molecular hydrogen, in conjunction with a specific electron acceptor, cytochrome c3.
CATALYTIC ACTIVITY: 2 H₂ + ferricytochrome c3 = 4 H⁺ + ferrocytochrome c3.
COFACTOR: Binds 2 4Fe-4S clusters.
COFACTOR: Binds 1 3Fe-4S cluster.
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.
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.

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

M58339; AAA23369.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A45865; A45865.

3D structure databases

PDB

1H2A; X-ray; 1.80 A; S=1-317.	[ExPASy / RCSB / EBI]
1H2R; X-ray; 1.40 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBH; X-ray; 1.35 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBJ; X-ray; 1.35 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBK; X-ray; 1.18 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBL; X-ray; 1.20 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBM; X-ray; 1.40 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBO; X-ray; 1.35 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBR; X-ray; 1.34 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBT; X-ray; 1.34 A; S=51-317.	[ExPASy / RCSB / EBI]
1UBU; X-ray; 1.35 A; S=51-317.	[ExPASy / RCSB / EBI]
1WUH; X-ray; 1.24 A; S=51-317.	[ExPASy / RCSB / EBI]
1WUI; X-ray; 1.04 A; S=51-317.	[ExPASy / RCSB / EBI]
1WUJ; X-ray; 1.40 A; S=51-317.	[ExPASy / RCSB / EBI]
1WUK; X-ray; 1.10 A; S=51-317.	[ExPASy / RCSB / EBI]
1WUL; X-ray; 1.50 A; S=51-317.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H2A; -.
1H2R; -.
1UBH; -.
1UBJ; -.
1UBK; -.
1UBL; -.
1UBM; -.
1UBO; -.
1UBR; -.
1UBT; -.
1UBU; -.
1WUH; -.
1WUI; -.
1WUJ; -.
1WUK; -.
1WUL; -.

ModBase

P21853.

Ontologies

GO:0009375;	Cellular component: ferredoxin hydrogenase complex (inferred from electronic annotation from InterPro).
GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047806;	Molecular function: cytochrome-c3 hydrogenase activity (inferred from electronic annotation from EC).
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 UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001821; NiFe_hyd_ssu.
IPR013634; NiFe_hyd_ssu_N.
IPR006137; OxRdtase_q6.
IPR006311; Tat.
Graphical view of domain structure.

Pfam

PF08425; NiFe_dehyd_N; 1.
PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000310; NiFe_hyd_ssu; 1.

PRINTS

PR00614; NIHGNASESMLL.

TIGRFAMs

TIGR00391; hydA; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

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

Other

P21853; -.

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

Keywords

3D-structure; 3Fe-4S; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 50`	`50`	`Tat-type signal.`
`CHAIN`	`51 317`	`267`	`Periplasmic [NiFe] hydrogenase small subunit.`	`PRO_0000013419`
`METAL`	`67 67`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`70 70`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`164 164`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`200 200`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`238 238`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen.`
`METAL`	`241 241`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`266 266`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`272 272`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`281 281`		`Iron-sulfur 3 (3Fe-4S).`
`METAL`	`299 299`		`Iron-sulfur 3 (3Fe-4S).`
`METAL`	`302 302`		`Iron-sulfur 3 (3Fe-4S).`
`STRAND`	`54 56`	`3`
`STRAND`	`58 65`	`8`
`HELIX`	`69 75`	`7`
`TURN`	`78 81`	`4`
`HELIX`	`82 87`	`6`
`STRAND`	`91 94`	`4`
`TURN`	`96 98`	`3`
`HELIX`	`103 115`	`13`
`STRAND`	`121 129`	`9`
`HELIX`	`132 134`	`3`
`STRAND`	`137 139`	`3`
`HELIX`	`144 151`	`8`
`HELIX`	`152 154`	`3`
`STRAND`	`155 162`	`8`
`HELIX`	`163 167`	`5`
`HELIX`	`170 172`	`3`
`HELIX`	`183 186`	`4`
`HELIX`	`188 190`	`3`
`STRAND`	`195 197`	`3`
`STRAND`	`199 201`	`3`
`HELIX`	`204 217`	`14`
`HELIX`	`230 233`	`4`
`STRAND`	`234 236`	`3`
`HELIX`	`238 240`	`3`
`HELIX`	`244 248`	`5`
`HELIX`	`259 262`	`4`
`HELIX`	`268 270`	`3`
`HELIX`	`274 276`	`3`
`HELIX`	`281 284`	`4`
`TURN`	`287 289`	`3`
`HELIX`	`292 295`	`4`
`HELIX`	`307 310`	`4`

Sequence information

Length: 317 AA [This is the length of the unprocessed precursor]

Molecular weight: 34113 Da [This is the MW of the unprocessed precursor]

CRC64: 2EAF2D471932C8A8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKISIGLGKE GVEERLAERG VSRRDFLKFC TAIAVTMGMG PAFAPEVARA LMGPRRPSVV 

        70         80         90        100        110        120 
YLHNAECTGC SESVLRAFEP YIDTLILDTL SLDYHETIMA AAGDAAEAAL EQAVNSPHGF 

       130        140        150        160        170        180 
IAVVEGGIPT AANGIYGKVA NHTMLDICSR ILPKAQAVIA YGTCATFGGV QAAKPNPTGA 

       190        200        210        220        230        240 
KGVNDALKHL GVKAINIAGC PPNPYNLVGT IVYYLKNKAA PELDSLNRPT MFFGQTVHEQ 

       250        260        270        280        290        300 
CPRLPHFDAG EFAPSFESEE ARKGWCLYEL GCKGPVTMNN CPKIKFNQTN WPVDAGHPCI 

       310 
GCSEPDFWDA MTPFYQN

P21853 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