[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=B10; DOI=10.1093/nar/18.17.5285; PubMed=2402452 [NCBI, ExPASy, EBI, Israel, Japan] Schneider C.G., Schmitt H.J., Schild C., Tichy H.V., Lotz W.; "DNA sequence encoding the two structural genes for the uptake hydrogenase of Rhizobium leguminosarum bv. viciae B10."; Nucleic Acids Res. 18:5285-5285(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=128c53; DOI=10.1007/BF00036924; PubMed=2103457 [NCBI, ExPASy, EBI, Israel, Japan] Hidalgo E., Leyva A., Ruiz-Argueso T.; "Nucleotide sequence of the hydrogenase structural genes from Rhizobium leguminosarum."; Plant Mol. Biol. 15:367-370(1990).

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.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not 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

Z36981; CAA85430.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52974; CAA37148.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11968; S11968.

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

P18637.

Ontologies

GO:0005886;	Cellular component: plasma membrane (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:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
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

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 46`	`46`	`Tat-type signal (Potential).`
`CHAIN`	`47 360`	`314`	`Uptake hydrogenase small subunit.`	`PRO_0000013434`
`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).`
`CONFLICT`	`160 160`		`C -> S (in Ref. 1; CAA85430).`
`CONFLICT`	`222 222`		`R -> P (in Ref. 1; CAA85430).`
`CONFLICT`	`228 230`		`SQR -> AQP (in Ref. 1; CAA85430).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 39149 Da [This is the MW of the unprocessed precursor]

CRC64: 85304E046F3DAAAF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAETFYDV IRRQGITRRS FTKFCSLTAA SLGFGPGAAT AMAEALETKE RVPVIWMHGL 

        70         80         90        100        110        120 
ECTCCSESFI RSAHPLVKDV VLSMISLDYD DTIMAAAGHQ AESILAETKE KYKGKYILAV 

       130        140        150        160        170        180 
EGNPPLNEGG MFCIDGGKPF VEKLKWMAED AMAIIAWGAC ASWGCVQAAK PNPTQATPID 

       190        200        210        220        230        240 
KVILDKPIIK VPGCPPIAEV MTGVVTFITT FGKLPELDRQ GRPKMFYSQR IHDKCYRRPH 

       250        260        270        280        290        300 
FDAGQFVEEW DDEGARKGYC LYKMGCKGPT TYNACSTVRW NGGVSFPIQS GHGCIGCSED 

       310        320        330        340        350        360 
GFWDNGSFYD RLTNIHQFGI EANADKVGMT AAGVVGGAIA AHAAVTAVKR LTTKREKADA

P18637 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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