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UniProtKB/Swiss-Prot entry P29166

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

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Entry information
Entry name PHF1_CLOPA
Primary accession number P29166
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Iron hydrogenase 1
Synonyms EC 1.12.7.2
[Fe] hydrogenase
Fe-only hydrogenase
CpI
Gene name None
From
Clostridium pasteurianum [TaxID: 1501] 
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
DOI=10.1021/bi00104a018; PubMed=1911757 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer J., Gagnon J.;
"Primary structure of hydrogenase I from Clostridium pasteurianum.";
Biochemistry 30:9697-9704(1991).
[2]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1126/science.282.5395.1853; PubMed=9836629 [NCBI, ExPASy, EBI, Israel, Japan]
Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C.;
"X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8-A resolution.";
Science 282:1853-1858(1998).
[3]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi9913193; PubMed=10529166 [NCBI, ExPASy, EBI, Israel, Japan]
Lemon B.J., Peters J.W.;
"Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.";
Biochemistry 38:12969-12973(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
M81737; AAA23248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40330; HQCL1P.
3D structure databases
PDB
1C4A; X-ray; 2.40 A; A=1-574.[ExPASy / RCSB / EBI]
1C4C; X-ray; 2.40 A; A=1-574.[ExPASy / RCSB / EBI]
1FEH; X-ray; 1.80 A; A=1-574.[ExPASy / RCSB / EBI]
3C8Y; X-ray; 1.39 A; A=1-574.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C4A; -.
1C4C; -.
1FEH; -.
3C8Y; -.
ModBase P29166.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
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 InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR004108; Fe_hydrogenase_lsu_C.
IPR003149; Fe_hydrogenase_ssu-like.
IPR013352; Fe_hydrogenase_subset.
IPR001041; Ferredoxin.
Graphical view of domain structure.
Gene3D G3DSA:4.10.260.20; Fe_hyd_ssu-like; 1.
Pfam PF02906; Fe_hyd_lg_C; 1.
PF02256; Fe_hyd_SSU; 1.
PF00111; Fer2; 1.
PF00037; Fer4; 2.
Pfam graphical view of domain structure.
PRINTS PR00353; 4FE4SFRDOXIN.
TIGRFAMs TIGR02512; Fe_only_hydrog; 1.
PROSITE PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29166.
ProtoNet P29166.
Other
DrugBank DB00916; Metronidazole.
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; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   574  574     Iron hydrogenase 1. PRO_0000199732
DOMAIN   1    78  78     2Fe-2S ferredoxin-type. 
DOMAIN   138   167  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   181   210  30     4Fe-4S ferredoxin-type 2. 
METAL   34    34        Iron-sulfur 1 (2Fe-2S). 
METAL   46    46        Iron-sulfur 1 (2Fe-2S). 
METAL   49    49        Iron-sulfur 1 (2Fe-2S). 
METAL   62    62        Iron-sulfur 1 (2Fe-2S). 
METAL   94    94        Iron-sulfur 2 (4Fe-4S); via tele nitrogen. 
METAL   98    98        Iron-sulfur 2 (4Fe-4S). 
METAL   101   101        Iron-sulfur 2 (4Fe-4S). 
METAL   107   107        Iron-sulfur 2 (4Fe-4S). 
METAL   147   147        Iron-sulfur 3 (4Fe-4S). 
METAL   150   150        Iron-sulfur 3 (4Fe-4S). 
METAL   153   153        Iron-sulfur 3 (4Fe-4S). 
METAL   157   157        Iron-sulfur 4 (4Fe-4S). 
METAL   190   190        Iron-sulfur 4 (4Fe-4S). 
METAL   193   193        Iron-sulfur 4 (4Fe-4S). 
METAL   196   196        Iron-sulfur 4 (4Fe-4S). 
METAL   200   200        Iron-sulfur 3 (4Fe-4S). 
METAL   300   300        Iron-sulfur 5 (4Fe-4S). 
METAL   355   355        Iron-sulfur 5 (4Fe-4S). 
METAL   499   499        Iron-sulfur 5 (4Fe-4S). 
METAL   503   503        Diiron subcluster. 
METAL   503   503        Iron-sulfur 5 (4Fe-4S). 
STRAND   2     6  5      
STRAND   9    13  5      
HELIX   19    25  7      
STRAND   42    44  3      
STRAND   50    53  4      
TURN   54    56  3      
STRAND   57    60  4      
HELIX   61    63  3      
STRAND   71    75  5      
HELIX   77    91  15      
TURN   102   105  4      
HELIX   108   116  9      
HELIX   129   132  4      
STRAND   137   143  7      
HELIX   144   146  3      
HELIX   152   161  10      
STRAND   166   171  6      
STRAND   174   179  6      
HELIX   180   182  3      
HELIX   185   187  3      
HELIX   195   199  5      
STRAND   205   207  3      
HELIX   211   219  9      
STRAND   224   229  6      
HELIX   231   235  5      
HELIX   237   241  5      
HELIX   250   260  11      
STRAND   263   267  5      
HELIX   268   289  22      
HELIX   301   310  10      
HELIX   312   317  6      
HELIX   324   332  9      
HELIX   335   338  4      
HELIX   344   346  3      
STRAND   347   354  8      
HELIX   357   362  6      
STRAND   367   369  3      
STRAND   372   374  3      
STRAND   376   380  5      
HELIX   381   390  10      
HELIX   395   397  3      
HELIX   405   407  3      
HELIX   412   415  4      
TURN   416   418  3      
HELIX   422   436  15      
HELIX   446   448  3      
STRAND   453   461  9      
STRAND   464   473  10      
HELIX   474   482  9      
HELIX   485   487  3      
STRAND   493   499  7      
HELIX   503   505  3      
HELIX   514   519  6      
HELIX   522   536  15      
HELIX   542   544  3      
HELIX   546   554  9      
HELIX   562   567  6      
Sequence information
Length: 574 AA [This is the length of the unprocessed precursor] Molecular weight: 63828 Da [This is the MW of the unprocessed precursor] CRC64: 17E28A74E23C7DEE [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKTIIINGVQ FNTDEDTTIL KFARDNNIDI SALCFLNNCN NDINKCEICT VEVEGTGLVT 

        70         80         90        100        110        120 
ACDTLIEDGM IINTNSDAVN EKIKSRISQL LDIHEFKCGP CNRRENCEFL KLVIKYKARA 

       130        140        150        160        170        180 
SKPFLPKDKT EYVDERSKSL TVDRTKCLLC GRCVNACGKN TETYAMKFLN KNGKTIIGAE 

       190        200        210        220        230        240 
DEKCFDDTNC LLCGQCIIAC PVAALSEKSH MDRVKNALNA PEKHVIVAMA PSVRASIGEL 

       250        260        270        280        290        300 
FNMGFGVDVT GKIYTALRQL GFDKIFDINF GADMTIMEEA TELVQRIENN GPFPMFTSCC 

       310        320        330        340        350        360 
PGWVRQAENY YPELLNNLSS AKSPQQIFGT ASKTYYPSIS GLDPKNVFTV TVMPCTSKKF 

       370        380        390        400        410        420 
EADRPQMEKD GLRDIDAVIT TRELAKMIKD AKIPFAKLED SEADPAMGEY SGAGAIFGAT 

       430        440        450        460        470        480 
GGVMEAALRS AKDFAENAEL EDIEYKQVRG LNGIKEAEVE INNNKYNVAV INGASNLFKF 

       490        500        510        520        530        540 
MKSGMINEKQ YHFIEVMACH GGCVNGGGQP HVNPKDLEKV DIKKVRASVL YNQDEHLSKR 

       550        560        570 
KSHENTALVK MYQNYFGKPG EGRAHEILHF KYKK
P29166 in FASTA format

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