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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1105/tpc.13.4.965; PubMed=11283349 [NCBI, ExPASy, EBI, Israel, Japan]
Frankenberg N.,
Mukougawa K.,
Kohchi T.,
Lagarias J.C.;
"Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms.";
Plant Cell 13:965-978(2001).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G.,
Larimer F.W.,
Lamerdin J.E.,
Malfatti S.,
Chain P.,
Ahlgren N.A.,
Arellano A.,
Coleman M.,
Hauser L.,
Hess W.R.,
Johnson Z.I.,
Land M.L.,
Lindell D.,
Post A.F.,
Regala W.,
Shah M.,
Shaw S.L.,
Steglich C.,
Sullivan M.B., ![]()
Ting C.S.,
Tolonen A.,
Webb E.A.,
Zinser E.R.,
Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(2003).
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- FUNCTION: Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge.
- CATALYTIC ACTIVITY: 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin.
- SIMILARITY: Belongs to the HY2 family.
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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: 236 AA [This is the length of the unprocessed precursor] |
Molecular weight: 28340 Da [This is the MW of the unprocessed precursor] |
CRC64: D4F215B59B1282D2 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MFESLKNFVK TNIEDLDGKE LEISKEFKEH HNKDSKYIIK NWIFESQQYR KWRITKLDGG
70 80 90 100 110 120
DKLQVFNTVA YPNFKSEFPI LGADILWFGT SQKLLAIFDY QPLIQEKKYL QKYCSSLDFI
130 140 150 160 170 180
KNQYSVFDNH KMKNIYDSKK YFSPWVMICR GNKLNLDRDL NNIFCSFVSN YLTINKLHQN
190 200 210 220 230
NQFLDLEQIK NNQIDYDKYS AEKDPADKLF KTFFGETWTE NFINNFLFTL NHNPLK
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Q93SN8 in FASTA format |
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