[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) OF 19-552. 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: Nickel.
COFACTOR: Iron.
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Periplasm.
MISCELLANEOUS: Perhaps the leader of the small subunit serves as a transport vehicle for both subunits.
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large 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; AAA23370.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B45865; B45865.

3D structure databases

PDB

1H2A; X-ray; 1.80 A; L=1-567.	[ExPASy / RCSB / EBI]
1H2R; X-ray; 1.40 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBH; X-ray; 1.35 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBJ; X-ray; 1.35 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBK; X-ray; 1.18 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBL; X-ray; 1.20 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBM; X-ray; 1.40 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBO; X-ray; 1.35 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBR; X-ray; 1.34 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBT; X-ray; 1.34 A; L=19-552.	[ExPASy / RCSB / EBI]
1UBU; X-ray; 1.35 A; L=19-552.	[ExPASy / RCSB / EBI]
1WUH; X-ray; 1.24 A; L=19-552.	[ExPASy / RCSB / EBI]
1WUI; X-ray; 1.04 A; L=19-552.	[ExPASy / RCSB / EBI]
1WUJ; X-ray; 1.40 A; L=19-552.	[ExPASy / RCSB / EBI]
1WUK; X-ray; 1.10 A; L=19-552.	[ExPASy / RCSB / EBI]
1WUL; X-ray; 1.50 A; L=19-552.	[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

P21852.

Ontologies

GO:0042597;	Cellular component: periplasmic space (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:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151;	Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001501; Ni-dep_hyd_lsu.
Graphical view of domain structure.

Pfam

PF00374; NiFeSe_Hases; 1.
Pfam graphical view of domain structure.

PROSITE

PS00507; NI_HGENASE_L_1; 1.
PS00508; NI_HGENASE_L_2; 1.

Other

P21852; -.

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

Keywords

3D-structure; Iron; Magnesium; Metal-binding; Nickel; Oxidoreductase; Periplasm.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 552`	`552`	`Periplasmic [NiFe] hydrogenase large subunit.`	`PRO_0000013405`
`PROPEP`	`553 567`	`15`		`PRO_0000013406`
`METAL`	`62 62`		`Magnesium.`
`METAL`	`81 81`		`Nickel.`
`METAL`	`84 84`		`Iron.`
`METAL`	`84 84`		`Nickel.`
`METAL`	`498 498`		`Magnesium; via carbonyl oxygen.`
`METAL`	`546 546`		`Nickel.`
`METAL`	`549 549`		`Iron.`
`METAL`	`549 549`		`Nickel.`
`METAL`	`552 552`		`Magnesium; via tele nitrogen.`
`STRAND`	`23 29`	`7`
`STRAND`	`32 35`	`4`
`STRAND`	`37 44`	`8`
`STRAND`	`47 55`	`9`
`HELIX`	`61 65`	`5`
`HELIX`	`70 72`	`3`
`HELIX`	`73 78`	`6`
`TURN`	`83 86`	`4`
`HELIX`	`87 100`	`14`
`HELIX`	`106 130`	`25`
`HELIX`	`133 135`	`3`
`HELIX`	`139 144`	`6`
`HELIX`	`147 157`	`11`
`STRAND`	`158 160`	`3`
`HELIX`	`164 179`	`16`
`HELIX`	`184 186`	`3`
`TURN`	`190 193`	`4`
`HELIX`	`202 230`	`29`
`STRAND`	`233 235`	`3`
`HELIX`	`247 250`	`4`
`HELIX`	`252 271`	`20`
`HELIX`	`273 283`	`11`
`HELIX`	`285 288`	`4`
`STRAND`	`296 298`	`3`
`HELIX`	`309 311`	`3`
`STRAND`	`312 314`	`3`
`STRAND`	`317 320`	`4`
`HELIX`	`332 334`	`3`
`STRAND`	`336 338`	`3`
`STRAND`	`344 347`	`4`
`HELIX`	`352 354`	`3`
`STRAND`	`371 373`	`3`
`STRAND`	`375 380`	`6`
`HELIX`	`387 396`	`10`
`HELIX`	`400 413`	`14`
`HELIX`	`417 420`	`4`
`HELIX`	`423 453`	`31`
`STRAND`	`467 477`	`11`
`STRAND`	`480 489`	`10`
`STRAND`	`492 499`	`8`
`HELIX`	`501 506`	`6`
`HELIX`	`517 521`	`5`
`TURN`	`522 524`	`3`
`STRAND`	`530 532`	`3`
`HELIX`	`534 542`	`9`
`HELIX`	`547 551`	`5`

Sequence information

Length: 567 AA [This is the length of the unprocessed precursor]

Molecular weight: 62627 Da [This is the MW of the unprocessed precursor]

CRC64: 6F9952506A11A211 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGCRAQNAP GGIPVTPKSS YSGPIVVDPV TRIEGHLRIE VEVENGKVKN AYSSSTLFRG 

        70         80         90        100        110        120 
LEIILKGRDP RDAQHFTQRT CGVCTYTHAL ASTRCVDNAV GVHIPKNATY IRNLVLGAQY 

       130        140        150        160        170        180 
LHDHIVHFYH LHALDFVDVT AALKADPAKA AKVASSISPR KTTAADLKAV QDKLKTFVET 

       190        200        210        220        230        240 
GQLGPFTNAY FLGGHPAYYL DPETNLIATA HYLEALRLQV KAARAMAVFG AKNPHTQFTV 

       250        260        270        280        290        300 
VGGVTCYDAL TPQRIAEFEA LWKETKAFVD EVYIPDLLVV AAAYKDWTQY GGTDNFITFG 

       310        320        330        340        350        360 
EFPKDEYDLN SRFFKPGVVF KRDFKNIKPF DKMQIEEHVR HSWYEGAEAR HPWKGQTQPK 

       370        380        390        400        410        420 
YTDLHGDDRY SWMKAPRYMG EPMETGPLAQ VLIAYSQGHP KVKAVTDAVL AKLGVGPEAL 

       430        440        450        460        470        480 
FSTLGRTAAR GIETAVIAEY VGVMLQEYKD NIAKGDNVIC APWEMPKQAE GVGFVNAPRG 

       490        500        510        520        530        540 
GLSHWIRIED GKIGNFQLVV PSTWTLGPRC DKNNVSPVEA SLIGTPVADA KRPVEILRTV 

       550        560 
HSFDPCIACG VHVIDGHTNE VHKFRIL

P21852 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