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UniProtKB/Swiss-Prot entry P13063


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PHSS_DESBA
Primary accession number P13063
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 74)
Name and origin of the protein
Protein name Periplasmic [NiFeSe] hydrogenase small subunit [Precursor]
Synonyms EC 1.12.99.6
NiFeSe hydrogenlyase small chain
Gene name None
From
Desulfovibrio baculatus (Desulfomicrobium baculatus) [TaxID: 899] 
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; Desulfomicrobiaceae; Desulfomicrobium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3316183 [NCBI, ExPASy, EBI, Israel, Japan]
Menon N.K., Peck H.D. Jr., le Gall J., Przybyla A.E.;
"Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus.";
J. Bacteriol. 169:5401-5407(1987).
[2]
ERRATUM, AND SEQUENCE REVISION.
Menon N.K., Pect H.D. Jr., le Gall J., Przybyla A.E.;
J. Bacteriol. 170:4429-4429(1988).
[3]
PROTEIN SEQUENCE OF 33-67.
STRAIN=DSM 1743;
DOI=10.1016/0006-291X(87)90376-7; PubMed=3322275 [NCBI, ExPASy, EBI, Israel, Japan]
Prickril B.C., He S.H., Li C., Menon N.K., Choi E.S., Przybyla A.E., Dervartanian D.V., Peck H.D. Jr., Fauque G., le Gall J., Teixeira M., Moura I., Moura J.J.G., Patil D., Huynh B.H.;
"Identification of three classes of hydrogenase in the genus, Desulfovibrio.";
Biochem. Biophys. Res. Commun. 149:369-377(1987).
[4]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
DOI=10.1016/S0969-2126(99)80072-0; PubMed=10378275 [NCBI, ExPASy, EBI, Israel, Japan]
Garcin E., Vernede X., Hatchikian E.C., Volbeda A., Frey M., Fontecilla-Camps J.-C.;
"The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center.";
Structure 7:557-566(1999).
Comments
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
M18271; AAA23376.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28380; HQDVSB.
3D structure databases
PDB
1CC1; X-ray; 2.15 A; S=33-315.[ExPASy / RCSB / EBI]
PDBsum 1CC1; -.
ModBase P13063.
Protein-protein interaction databases
DIP DIP:6126N; -.
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).
BLOCKS P13063.
Other
ProtoNet P13063.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    32  32     Tat-type signal. 
CHAIN   33   315  283     Periplasmic [NiFeSe] hydrogenase small subunit. PRO_0000013420
METAL   50    50        Iron-sulfur 1 (4Fe-4S). 
METAL   53    53        Iron-sulfur 1 (4Fe-4S). 
METAL   158   158        Iron-sulfur 1 (4Fe-4S). 
METAL   196   196        Iron-sulfur 1 (4Fe-4S). 
METAL   240   240        Iron-sulfur 2 (4Fe-4S); via pros nitrogen. 
METAL   243   243        Iron-sulfur 2 (4Fe-4S). 
METAL   263   263        Iron-sulfur 2 (4Fe-4S). 
METAL   269   269        Iron-sulfur 2 (4Fe-4S). 
METAL   278   278        Iron-sulfur 3 (4Fe-4S). 
METAL   290   290        Iron-sulfur 3 (4Fe-4S). 
METAL   296   296        Iron-sulfur 3 (4Fe-4S). 
METAL   299   299        Iron-sulfur 3 (4Fe-4S). 
STRAND   40    48  9      
HELIX   52    58  7      
TURN   61    64  4      
HELIX   65    71  7      
STRAND   73    77  5      
TURN   79    81  3      
HELIX   86    99  14      
TURN   100   102  3      
STRAND   103   113  11      
HELIX   115   118  4      
STRAND   121   124  4      
STRAND   131   133  3      
HELIX   138   145  8      
HELIX   146   148  3      
STRAND   149   156  8      
HELIX   157   161  5      
HELIX   164   166  3      
HELIX   177   184  8      
STRAND   190   193  4      
HELIX   200   215  16      
TURN   217   219  3      
HELIX   232   235  4      
STRAND   236   238  3      
TURN   239   242  4      
HELIX   246   250  5      
STRAND   260   264  5      
HELIX   265   267  3      
HELIX   271   273  3      
HELIX   278   281  4      
TURN   284   287  4      
HELIX   290   293  4      
TURN   302   305  4      
HELIX   306   308  3      
Sequence information
Length: 315 AA [This is the length of the unprocessed precursor] Molecular weight: 34221 Da [This is the MW of the unprocessed precursor] CRC64: A3C592F12B95ED83 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLSRREFVK LCSAGVAGLG ISQIYHPGIV HAMTEGAKKA PVIWVQGQGC TGCSVSLLNA 

        70         80         90        100        110        120 
VHPRIKEILL DVISLEFHPT VMASEGEMAL AHMYEIAEKF NGNFFLLVEG AIPTAKEGRY 

       130        140        150        160        170        180 
CIVGETLDAK GHHHEVTMME LIRDLAPKSL ATVAVGTCSA YGGIPAAEGN VTGSKSVRDF 

       190        200        210        220        230        240 
FADEKIEKLL VNVPGCPPHP DWMVGTLVAA WSHVLNPTEH PLPELDDDGR PLLFFGDNIH 

       250        260        270        280        290        300 
ENCPYLDKYD NSEFAETFTK PGCKAELGCK GPSTYADCAK RRWNNGINWC VENAVCIGCV 

       310 
EPDFPDGKSP FYVAE 

P13063 in FASTA format

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