[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2661538 [NCBI, ExPASy, EBI, Israel, Japan] Voordouw G., Strang J.D., Wilson F.R.; "Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello."; J. Bacteriol. 171:3881-3889(1989).

Comments

FUNCTION: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
CATALYTIC ACTIVITY: H₂ + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H⁺.
COFACTOR: Binds 3 4Fe-4S clusters per subunit (By similarity).
COFACTOR: Binds 2 iron ions per subunit (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Periplasm.
MISCELLANEOUS: [Fe], [NiFe], and [NiFeSe] hydrogenases appear to represent three distinct enzymes having hydrogenase activity.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

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

M27212; AAA23373.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32886; HQDVLV.

3D structure databases

HSSP

P07598; 1HFE. [HSSP ENTRY / PDB]

SMR

P13629; 2-397.

ModBase

P13629.

Ontologies

GO:0042597;	Cellular component: periplasmic space (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:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR004108; Fe_hydrogenase_lsu_C.
IPR013352; Fe_hydrogenase_subset.
Graphical view of domain structure.

Pfam

PF02906; Fe_hyd_lg_C; 1.
PF00037; Fer4; 2.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.

TIGRFAMs

TIGR02512; Fe_only_hydrog; 1.

PROSITE

PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Repeat; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 421`	`421`	`Periplasmic [Fe] hydrogenase large subunit.`	`PRO_0000159240`
`DOMAIN`	`26 55`	`30`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`56 86`	`31`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`35 35`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`38 38`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`41 41`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`45 45`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`66 66`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`69 69`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`72 72`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`76 76`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`179 179`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`234 234`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`378 378`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`382 382`		`Diiron subcluster (By similarity).`
`METAL`	`382 382`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 46279 Da [This is the MW of the unprocessed precursor]

CRC64: 8E987ABC4DC7C965 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRIEMEKIF YEDHAPDPKA DPDKLFFIQI DESKCIGCDS CQQYCPTGAI FGDTGDAHKI 

        70         80         90        100        110        120 
PHEELCINCG QCLTHCPVGA IYESQSWVTE IEKKIKAKDV KVIAMPAPAV RYALGDAFGL 

       130        140        150        160        170        180 
PVGTVTTGKM FSALKELGFD HCWDNEFTAD VTIWEEGTEF VQRLTKKLDK PLPQFTSCCP 

       190        200        210        220        230        240 
GWHKYVESLY PELFPHMSSC KSPIGMLGTL AKTYGADRMK YDRAKVYTVS IMPCTAKKYE 

       250        260        270        280        290        300 
GMRPQLWDSG HKDIDATIDT RELAYMIKKA KIDFTKLPDG KRDTLMGEST GGATLFGVTG 

       310        320        330        340        350        360 
GVMEAALRYA YQAVTGKKPE SMDFKGVRGL QGVKEATVNV GGVDVKVAVV HGARRFHDVC 

       370        380        390        400        410        420 
ELVKAGKAPW HFIEFMACPG GCVCGGGQPV MPGVLEAADR RSTRMYAGLK KRLAMASASR 


A

P13629 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