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[1]
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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).
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[2]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
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).
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[3]
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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).
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 317 AA [This is the length of the unprocessed precursor] |
Molecular weight: 34113 Da [This is the MW of the unprocessed precursor] |
CRC64: 2EAF2D471932C8A8 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKISIGLGKE GVEERLAERG VSRRDFLKFC TAIAVTMGMG PAFAPEVARA LMGPRRPSVV
70 80 90 100 110 120
YLHNAECTGC SESVLRAFEP YIDTLILDTL SLDYHETIMA AAGDAAEAAL EQAVNSPHGF
130 140 150 160 170 180
IAVVEGGIPT AANGIYGKVA NHTMLDICSR ILPKAQAVIA YGTCATFGGV QAAKPNPTGA
190 200 210 220 230 240
KGVNDALKHL GVKAINIAGC PPNPYNLVGT IVYYLKNKAA PELDSLNRPT MFFGQTVHEQ
250 260 270 280 290 300
CPRLPHFDAG EFAPSFESEE ARKGWCLYEL GCKGPVTMNN CPKIKFNQTN WPVDAGHPCI
310
GCSEPDFWDA MTPFYQN
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P21853 in FASTA format |
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