[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 33303 / B10; DOI=10.1007/BF00340186; PubMed=3067084 [NCBI, ExPASy, EBI, Israel, Japan] Leclerc M., Colbeau A., Cauvin B., Vignais P.M.; "Cloning and sequencing of the genes encoding the large and the small subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus."; Mol. Gen. Genet. 214:97-107(1988).
[2]	ERRATUM, AND SEQUENCE REVISION. Leclerc M., Colbeau A., Cauvin B., Vignais P.M.; Mol. Gen. Genet. 215:368-368(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18. STRAIN=ATCC 33303 / B10; PubMed=8497190 [NCBI, ExPASy, EBI, Israel, Japan] Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C., Delphin C., Smith R.L., Chabert J., Vignais P.M.; "Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants."; Mol. Microbiol. 8:15-29(1993).

Comments

FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
CATALYTIC ACTIVITY: H₂ + A = AH₂.
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 2 4Fe-4S clusters (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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

X13520; CAA31869.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37261; AAA69668.1; ALT_TERM; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S08316; S08316.

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

P15283.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR001821; NiFe_hyd_ssu.
IPR013634; NiFe_hyd_ssu_N.
IPR006137; OxRdtase_q6.
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.

TIGR00391; hydA; 1.

Other

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

Keywords

3Fe-4S; 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 45`	`45`
`CHAIN`	`46 358`	`313`	`Uptake hydrogenase small subunit.`	`PRO_0000013435`
`METAL`	`62 62`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`65 65`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`160 160`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`194 194`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`232 232`		`Iron-sulfur 2 (4Fe-4S) (via pros nitrogen) (By similarity).`
`METAL`	`235 235`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`260 260`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`266 266`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`275 275`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`294 294`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`297 297`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 39403 Da [This is the MW of the unprocessed precursor]

CRC64: D08C1887F1376237 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDIETFYDV MRRQGITRRS FMKSVRSPQH VLGLGPSFVP KIGEAMETKP RTPVVWVHGL 

        70         80         90        100        110        120 
ECTCCSESFI RSAHPLAKDV VLSMISLDYD DTLMAAAGHA AEAAFEETIA KYKGNYILAV 

       130        140        150        160        170        180 
EGNPPLNEDG MFCITGGKPF VEKLRHAAEG AKAIISWGAC ASYGCVQAAA PNPTQATPVH 

       190        200        210        220        230        240 
KVITDKPIIK VPGCPPIAEV MTGVITYMLT FDRMPELDRQ GRPAMFYSQR IHDKCYRRPH 

       250        260        270        280        290        300 
FDAGQFVEHW DDENARKGYC LYKMGCKGPT TYNACSTVPL ERRRHFPIQS GHGCIGCSED 

       310        320        330        340        350 
GFWDQGSFYD RLTTIKQFGI EATADQIGWT ATGLVGAAVA AHAAVSVLKR AQKKNEEA

P15283 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