Sulfite reductase [NADPH] subunit beta (P47169)

Identification
NameSulfite reductase [NADPH] subunit beta
Synonyms
  • Extracellular mutant protein 17
Gene NameECM17
Enzyme Class
Biological Properties
General FunctionInvolved in iron ion binding
Specific FunctionCatalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate
Cellular LocationCytoplasm
SMPDB Pathways
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Sulfur metabolismec00920 Map00920
SMPDB Reactions
Sulfite + NADPH + hydron → water + NADP + Hydrogen sulfide
KEGG Reactions
NADP + water + Hydrogen sulfide ↔ hydron + Sulfite + NADPH
Metabolites
YMDB IDNameView
YMDB00114SulfiteShow
YMDB00121SulfideShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00653Hydrogen sulfideShow
YMDB00862hydronShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
binding
nucleotide binding
FMN binding
ion binding
cation binding
metal ion binding
transition metal ion binding
iron ion binding
metal cluster binding
iron-sulfur cluster binding
oxidoreductase activity
heme binding
catalytic activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome LocationNot Available
LocusYJR137C
Gene Sequence>4329 bp ATGACTGCTTCTGACCTCTTGACGCTCCCACAATTGTTGGCGCAATATTCCTCTAGTGCT CCCCAAAATAAAGTGTTCTACACTACTAGCACAAAAAATAGTCATTCATCCTTCAAAGGG CTAGAATCTGTTGCCACAGATGCTACTCATCTATTGAACAATCAAGATCCATTGAATACC ATCAAAGATCAACTCTCTAAGGACATTTTAACTACCGTTTTTACAGATGAAACTACTTTG GTCAAATCCATCCACCATCTATATTCTCTTCCTAATAAACTTCCATTGGTGATTACAGTG GATTTGAATTTGCAAGATTATTCCGCAATTCCTGCGTTAAAGGATCTTTCTTTCCCCATC TTAATATCTTCTGATTTGCAAACTGCAATTTCAAACGCGGACTCTTCTTATAAGATTGCT ACAAGTTCTCTGACCCCAGTTTTCCATTTTCTTAACTTGGAGAAAATTGGCACGAGTACA GCTATTGAACAAGACATCGACTTTCCTACCTTGGAGATTGCTAACGAAGAGACTAAAGTA GCATTATCAGAAGCTACTGATTCATTGACAAATTTTGAACTGGTTAAAGGTAAAGAGTCA ATTACCACTGTCATTGTTAACCTGTCACCATATGACGCGGAATTCAGTAGCGTATTGCCT TCAAACGTAGGATTGATCAAGATTAGAGTATACAGACCATGGAATTTTTCCAAGTTCTTG GAAATACTGCCATCTTCTGTTACCAAAATCGCCGTTTTACAGGGTGTCTCTAAGAAATCG CAATCAAACGAATTTCAACCATTTCTTTTGGACTTCTTTGGCAATTTTAATGAATTAGTT TCTAGGAACATCGAGCAGGTAGTGTTGACTAATATTGGTAATGTGAATGATTATGGCAAC GTTATCAACACCGTCATATCGAATATTAACAAGAAGGAACCAGATAATAACTTATTTTTA GGTGAATCCAATGAAAAGGCTGAGGAACAAGCTGAAGTTACTCAACTTATTTCTTCTGTC AAAAAAGTTGTGAACTTAGAAGACGCCTATATCAAAGTGCTAAAACAGTTATTTTCATCA AATCTACAAATTTTGAATCAATTTTCCAGTGAGACAATTGAACCAAGTAATCCAGAATTT GGTTTTGGACGCTTTTTAAAACAAGAAGCCCAGCGTGAAGAATTGATCAGCTTAGCAAAA ACCTCTCTTGATCCAAGTCTTTACTTGTCCGAGGATGCAAATAAAATTGTTCAACTATTA TCTAAATGGTTGTCATTCAATGGACGCGATCTTGACGAAGCTCAATTACAAGAGGCCAAT GCGACAGGTTTGGAAATATTTCAGTTATTACAATCTAATCAAGATTCCTCTACTGTCTTA AAATTCTTAAAGATAGCTCCAACAAGCGATTCTTTTATTTTCAAATCAAGCTGGCTAATT GGCTCCGATGCCTGGTCTTATGATTTGGGTCACTCAGGTATTCAACAGGTTTTATCCTCC CGTAAAAACATTAATGTTTTATTGATTGATTCAGAGCCATATGACCATAGAAAGCAAAAC CAGGATAGAAAGAAAGATGTTGGTTTGTACGCCATGAATTATTACAGTGCCTATGTTGCC TCTGTAGCAGTATATGCTTCTTACACCCAACTATTGACTGCAATAATAGAGGCATCTAAA TACAATGGTCCTTCTATTGTCTTGGCTTATTTGCCGTATAATTCCGAAAATGATACTCCA TTAGAAGTCTTAAAGGAAACCAAAAACGCCGTTGAATCTGGTTACTGGCCATTGTATAGG TTTAATCCTGTTTATGACGATCCATCAACAGATAAGGAGGCATTTAGCTTGGATTCTTCG GTTATCAGAAAACAATTACAGGACTTCTTAGACCGTGAGAATAAGCTTACCCTATTAACC AGAAAAGATCCATCTTTGTCAAGAAATCTAAAGCAATCTGCTGGTGATGCGTTGACAAGG AAACAAGAAAAAAGAAGCAAGGCTGCCTTCGATCAGTTATTGGAGGGTTTGTCCGGCCCA CCGCTACACGTCTATTATGCTTCTGACGGTGGTAATGCTGCAAACTTGGCAAAGAGACTA GCAGCAAGGGCATCTGCAAGAGGTTTAAAGGCTACTGTTCTGTCCATGGATGACATTATT TTGGAAGAATTACCTGGTGAAGAGAATGTAGTTTTCATTACTTCCACGGCTGGGCAAGGT GAATTCCCCCAAGACGGTAAGTCTTTCTGGGAAGCTCTGAAAAATGACACCGACTTGGAT TTAGCTAGTTTGAATGTTGCTGTTTTTGGTCTCGGTGATTCTGAGTATTGGCCACGTAAA GAAGATAAACATTATTTTAACAAGCCTTCACAGGATTTATTTAAGCGCTTGGAATTATTG AGTGCCAAAGCCCTAATTCCCTTGGGACTGGGTGATGATCAAGATGCTGATGGTTTCCAA ACTGCTTATTCTGAGTGGGAACCTAAATTATGGGAAGCTCTTGGTGTTTCCGGCGCTGCT GTTGATGATGAGCCAAAACCTGTTACAAACGAGGATATTAAGAGAGAATCTAATTTCTTG AGAGGTACTATCAGTGAGAACTTAAAGGATACTTCTTCAGGTGGTGTTACTCACGCTAAT GAACAATTAATGAAATTTCACGGTATTTACACCCAAGACGATCGTGACATTAGAGAAATA CGTAAGTCACAAGGCTTAGAGCCATACTATATGTTTATGGCAAGAGCTCGTTTACCAGGT GGTAAGACCACTCCACAACAATGGCTTGCTCTGGATCACTTATCTGATACTTCAGGCAAT GGTACCCTGAAATTAACAACAAGGGCAACCTTCCAGATTCATGGTGTGCTAAAGAAGAAC TTGAAACACACATTGAGAGGAATGAATGCAGTTCTTATGGATACATTAGCTGCTGCAGGT GACGTGAACAGAAATGTCATGGTTTCTGCTCTACCAACCAATGCCAAGGTTCACCAACAA ATCGCTGATATGGGAAAATTGATTTCTGATCATTTCTTACCAAAGACTACGGCCTACCAC GAAGTTTGGCTGGAGGGCCCAGAAGAACAGGACGATGATCCATCCTGGCCATCTATTTTT GAAAACAGAAAAGATGGTCCAAGAAAAAAGAAGACTCTAGTTAGCGGTAACGCTTTGGTC GATATTGAACCAATTTACGGTCCAACTTATCTGCCAAGAAAGTTTAAATTCAACATCGCC GTTCCTCCATATAACGATGTGGATGTATTATCTATCGATGTCGGTTTAGTTGCTATAGTT AACCCAGAAACTCAAATCGTGGAGGGTTATAATGTTTTTGTTGGTGGTGGTATGGGTACC ACTCATAACAACAAGAAAACTTACCCAAGATTAGGGTCATGCTTAGGTTTTGTTAAAACT GAAGACATTATTCCACCACTTGAAGGTATCGTTATTGTCCAAAGAGATCACGGTGACCGT AAAGACCGTAAGCATGCTCGTTTAAAGTATACTGTAGATGATATGGGTGTCGAAGGCTTC AAGCAAAAAGTGGAGGAATACTGGGGTAAGAAATTCGAGCCTGAGAGACCATTTGAGTTT AAATCTAATATTGATTACTTTGGATGGATTAAAGATGAAACTGGGTTAAACCACTTTACC GCATTTATTGAAAATGGTAGGGTTGAAGATACACCAGATTTGCCTCAAAAGACAGGTATT AGAAAGGTTGCTGAATACATGCTTAAGACTAATTCTGGTCATTTCAGATTGACTGGTAAT CAACATTTGGTTATCTCTAATATTACAGATGAACATGTTGCTGGAATAAAATCTATTTTA AAGACCTATAAATTGGATAACACCGATTTCAGCGGTTTGAGATTATCTTCATCTTCCTGT GTTGGTTTGCCAACATGTGGTTTAGCGTTTGCCGAATCTGAACGTTTCCTACCTGACATT ATTACTCAGTTGGAAGATTGTTTAGAAGAGTATGGTTTACGCCATGATTCCATTATTATG AGAATGACTGGTTGCCCTAACGGTTGTTCTCGTCCATGGCTAGGTGAATTAGCTCTTGTT GGTAAAGCTCCACATACTTATAACTTGATGCTTGGTGGTGGTTACCTCGGCCAAAGGCTA AACAAATTGTATAAGGCCAATGTGAAGGATGAGGAAATTGTCGACTACATCAAACCATTG TTTAAAAGGTATGCTTTAGAAAGAGAAGAAGGGGAACACTTTGGTGATTTCTGTATAAGA GTAGGTATCATTAAACCAACCACCGAGGGTAAATACTTCCATGAAGATGTGTCTGAAGAT GCCTATTAA
Protein Properties
Pfam Domain Function
Protein Residues1442
Protein Molecular Weight161218.0
Protein Theoretical pI5.15
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Sulfite reductase [NADPH] subunit beta MTASDLLTLPQLLAQYSSSAPQNKVFYTTSTKNSHSSFKGLESVATDATHLLNNQDPLNT IKDQLSKDILTTVFTDETTLVKSIHHLYSLPNKLPLVITVDLNLQDYSAIPALKDLSFPI LISSDLQTAISNADSSYKIATSSLTPVFHFLNLEKIGTSTAIEQDIDFPTLEIANEETKV ALSEATDSLTNFELVKGKESITTVIVNLSPYDAEFSSVLPSNVGLIKIRVYRPWNFSKFL EILPSSVTKIAVLQGVSKKSQSNEFQPFLLDFFGNFNELVSRNIEQVVLTNIGNVNDYGN VINTVISNINKKEPDNNLFLGESNEKAEEQAEVTQLISSVKKVVNLEDAYIKVLKQLFSS NLQILNQFSSETIEPSNPEFGFGRFLKQEAQREELISLAKTSLDPSLYLSEDANKIVQLL SKWLSFNGRDLDEAQLQEANATGLEIFQLLQSNQDSSTVLKFLKIAPTSDSFIFKSSWLI GSDAWSYDLGHSGIQQVLSSRKNINVLLIDSEPYDHRKQNQDRKKDVGLYAMNYYSAYVA SVAVYASYTQLLTAIIEASKYNGPSIVLAYLPYNSENDTPLEVLKETKNAVESGYWPLYR FNPVYDDPSTDKEAFSLDSSVIRKQLQDFLDRENKLTLLTRKDPSLSRNLKQSAGDALTR KQEKRSKAAFDQLLEGLSGPPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDII LEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDTDLDLASLNVAVFGLGDSEYWPRK EDKHYFNKPSQDLFKRLELLSAKALIPLGLGDDQDADGFQTAYSEWEPKLWEALGVSGAA VDDEPKPVTNEDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREI RKSQGLEPYYMFMARARLPGGKTTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKN LKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIADMGKLISDHFLPKTTAYH EVWLEGPEEQDDDPSWPSIFENRKDGPRKKKTLVSGNALVDIEPIYGPTYLPRKFKFNIA VPPYNDVDVLSIDVGLVAIVNPETQIVEGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKT EDIIPPLEGIVIVQRDHGDRKDRKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERPFEF KSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRKVAEYMLKTNSGHFRLTGN QHLVISNITDEHVAGIKSILKTYKLDNTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDI ITQLEDCLEEYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRL NKLYKANVKDEEIVDYIKPLFKRYALEREEGEHFGDFCIRVGIIKPTTEGKYFHEDVSED AY
References
External Links
ResourceLink
Saccharomyces Genome Database ECM17
Uniprot IDP47169
Uniprot NameECM17_YEAST
GenBank Gene IDZ49637
Genebank Protein ID1015876
General Reference
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Kobayashi, K., Yoshimoto, A. (1982). "Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics." Biochim Biophys Acta 705:348-356.6751400
  • Shevchenko, A., Jensen, O. N., Podtelejnikov, A. V., Sagliocco, F., Wilm, M., Vorm, O., Mortensen, P., Shevchenko, A., Boucherie, H., Mann, M. (1996). "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels." Proc Natl Acad Sci U S A 93:14440-14445.8962070
  • Lussier, M., White, A. M., Sheraton, J., di Paolo, T., Treadwell, J., Southard, S. B., Horenstein, C. I., Chen-Weiner, J., Ram, A. F., Kapteyn, J. C., Roemer, T. W., Vo, D. H., Bondoc, D. C., Hall, J., Zhong, W. W., Sdicu, A. M., Davies, J., Klis, F. M., Robbins, P. W., Bussey, H. (1997). "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae." Genetics 147:435-450.9335584
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956