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UniProtKB/Swiss-Prot entry P13065

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

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Entry information
Entry name PHSL_DESBA
Primary accession number P13065
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on February 26, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 72)
Name and origin of the protein
Protein name Periplasmic [NiFeSe] hydrogenase large subunit
Synonyms EC 1.12.99.6
NiFeSe hydrogenlyase large 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]
 X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SELENOCYSTEINE AT SEC-493.
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; AAA23375.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A33101; HQDVLB.
3D structure databases
PDB
1CC1; X-ray; 2.15 A; L=1-499.[ExPASy / RCSB / EBI]
PDBsum 1CC1; -.
ModBase P13065.
Protein-protein interaction databases
DIP DIP:6125N; -.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (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:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0008430; Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet P13065.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Iron; Metal-binding; Nickel; Oxidoreductase; Periplasm; Selenium; Selenocysteine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   514  513     Periplasmic [NiFeSe] hydrogenase large subunit. PRO_0000199704
METAL   52    52        Iron 2. 
METAL   71    71        Nickel. 
METAL   74    74        Iron 1. 
METAL   74    74        Nickel. 
METAL   445   445        Iron 2; via carbonyl oxygen. 
METAL   493   493        Nickel. 
METAL   496   496        Iron 1. 
METAL   496   496        Nickel. 
METAL   499   499        Iron 2. 
NON_STD   493   493        Selenocysteine. 
STRAND   14    19  6      
STRAND   22    25  4      
STRAND   27    34  8      
STRAND   37    45  9      
HELIX   51    54  4      
TURN   55    57  3      
HELIX   60    62  3      
HELIX   63    66  4      
HELIX   67    70  4      
STRAND   72    74  3      
HELIX   75    90  16      
HELIX   96   120  25      
HELIX   123   125  3      
HELIX   145   148  4      
HELIX   152   184  33      
STRAND   185   189  5      
STRAND   191   194  4      
STRAND   197   200  4      
HELIX   204   223  20      
HELIX   225   235  11      
HELIX   237   240  4      
STRAND   249   251  3      
STRAND   254   258  5      
STRAND   264   266  3      
STRAND   269   272  4      
STRAND   275   277  3      
HELIX   281   283  3      
STRAND   284   287  4      
STRAND   296   299  4      
HELIX   303   305  3      
STRAND   323   326  4      
HELIX   335   342  8      
HELIX   348   358  11      
HELIX   365   372  8      
HELIX   375   399  25      
STRAND   414   424  11      
STRAND   427   436  10      
STRAND   439   447  9      
HELIX   449   452  4      
HELIX   464   469  6      
HELIX   481   489  9      
HELIX   494   498  5      
Sequence information
Length: 514 AA [This is the length of the unprocessed precursor] Molecular weight: 56862 Da [This is the MW of the unprocessed precursor] CRC64: AC920132081C1ADC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSQAATPAAD GKVKISIDPL TRVEGHLKIE VEVKDGKVVD AKCSGGMFRG FEQILRGRDP 

        70         80         90        100        110        120 
RDSSQIVQRI CGVCPTAHCT ASVMAQDDAF GVKVTTNGRI TRNLIFGANY LQSHILHFYH 

       130        140        150        160        170        180 
LAALDYVKGP DVSPFVPRYA NADLLTDRIK DGAKADATNT YGLNQYLKAL EIRRICHEMV 

       190        200        210        220        230        240 
AMFGGRMPHV QGMVVGGATE IPTADKVAEY AARFKEVQKF VIEEYLPLIY TLGSVYTDLF 

       250        260        270        280        290        300 
ETGIGWKNVI AFGVFPEDDD YKTFLLKPGV YIDGKDEEFD SKLVKEYVGH SFFDHSAPGG 

       310        320        330        340        350        360 
LHYSVGETNP NPDKPGAYSF VKAPRYKDKP CEVGPLARMW VQNPELSPVG QKLLKELYGI 

       370        380        390        400        410        420 
EAKKFRDLGD KAFSIMGRHV LVAEETWLTA VAVEKWLKQV QPGAETYVKS EIPDAAEGTG 

       430        440        450        460        470        480 
FTEAPRGALL HYLKIKDKKI ENYQIVSATL WNANPRDDMG QRGPIEEALI GVPVPDIKNP 

       490        500        510 
VNVGRLVRSY DPULGCAVHV LHAETGEEHV VNID
P13065 in FASTA format

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