NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-63.
STRAIN=CH5 / OM5 / DSM 1227;
PubMed=9324252 [NCBI, ExPASy, EBI, Israel, Japan]
Santiago B., Meyer O.;
"Purification and molecular characterization of the H2 uptake membrane-bound NiFe-hydrogenase from the carboxidotrophic bacterium Oligotropha carboxidovorans.";
J. Bacteriol. 179:6053-6060(1997).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CH5 / OM5 / DSM 1227;
DOI=10.1016/j.gene.2003.08.027; PubMed=14644498 [NCBI, ExPASy, EBI, Israel, Japan]
Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
"Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H(2) and CO(2).";
Gene 322:67-75(2003).

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 (By similarity).
CATALYTIC ACTIVITY: H₂ + A = AH₂.
COFACTOR: Binds 2 4Fe-4S clusters.
COFACTOR: Binds 1 3Fe-4S cluster.
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 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

X82447; CAG28468.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

O33405.

Ontologies

GO:0009375;	Cellular component: ferredoxin hydrogenase complex (inferred from electronic annotation from InterPro).
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:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
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).
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

ProtoNet

O33405.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 45`	`45`	`Tat-type signal.`
`CHAIN`	`46 360`	`315`	`Uptake hydrogenase small subunit.`	`PRO_0000013433`
`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`	`62 62`		`C -> E (in Ref. 1; AA sequence).`

Sequence information

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

Molecular weight: 39322 Da [This is the MW of the unprocessed precursor]

CRC64: F4D5CB57BC1D1DA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTPTETFYEV MRRQGVTRRS FLKFCSLTAT ALGLGPAYTS EIAHAMETKP RTPVLWLHGL 

        70         80         90        100        110        120 
ECTCCSESFI RSAHPLVKDV VLSMISLDYD DTLMAAAGHQ AEAALADTIE RYKGNYILAV 

       130        140        150        160        170        180 
EGNPPLNEDG MFCIIGGKPF VDQLRYAAKH AKAIISWGSC ASHGCVQAAR PNPTRATPVH 

       190        200        210        220        230        240 
QVITDKPIIK VPGCPPIAEV MTGVITYMLT FGKLPELDRT GRPKMFYSQR IHDKCYRRPH 

       250        260        270        280        290        300 
FDAGQFVESF DDEGARRGYC LYKVGCKGPT TYNACSTIRW NEGTSFPIQA GHGCIGCSEE 

       310        320        330        340        350        360 
GFWDKGSWYA RLQDIHQFGI EANADQIGGT VAVGAAGAVA AHAAVSALKR AQTKRQTTTS

O33405 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