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Protein

Sulfite reductase [NADPH] subunit beta

Gene

MET5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate.

Catalytic activityi

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH.

Cofactori

Protein has several cofactor binding sites:
  • sirohemeBy similarityNote: Binds 1 siroheme per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes hydrogen sulfide from sulfite (NADPH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Sulfite reductase [NADPH] flavoprotein component (MET10), Sulfite reductase [NADPH] subunit beta (MET5)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes hydrogen sulfide from sulfite (NADPH route), the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1300 – 13001Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1306 – 13061Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1345 – 13451Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1349 – 13491Iron (siroheme axial ligand)By similarity
Metal bindingi1349 – 13491Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

  • cysteine biosynthetic process Source: UniProtKB-KW
  • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  • methionine biosynthetic process Source: UniProtKB-KW
  • sulfate assimilation Source: SGD
  • sulfur amino acid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis, Methionine biosynthesis

Keywords - Ligandi

4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-22.
UniPathwayiUPA00140; UER00207.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] subunit beta (EC:1.8.1.2)
Alternative name(s):
Extracellular mutant protein 17
Gene namesi
Name:MET5
Synonyms:ECM17
Ordered Locus Names:YJR137C
ORF Names:J2126
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR137C.
SGDiS000003898. MET5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • sulfite reductase complex (NADPH) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14421442Sulfite reductase [NADPH] subunit betaPRO_0000199968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei903 – 9031PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47169.
PeptideAtlasiP47169.

PTM databases

iPTMnetiP47169.

Interactioni

Subunit structurei

Alpha(2)-beta2. The alpha component is a flavoprotein, the beta component is a hemoprotein.

Protein-protein interaction databases

BioGridi33893. 42 interactions.
IntActiP47169. 8 interactions.
MINTiMINT-4492135.

Structurei

3D structure databases

ProteinModelPortaliP47169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini682 – 831150Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000167149.
InParanoidiP47169.
KOiK00381.
OMAiSTTAYHE.
OrthoDBiEOG7DVDK9.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
3.90.480.10. 2 hits.
InterProiIPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
PR00397. SIROHAEM.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
SSF55124. SSF55124. 2 hits.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
PS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASDLLTLP QLLAQYSSSA PQNKVFYTTS TKNSHSSFKG LESVATDATH
60 70 80 90 100
LLNNQDPLNT IKDQLSKDIL TTVFTDETTL VKSIHHLYSL PNKLPLVITV
110 120 130 140 150
DLNLQDYSAI PALKDLSFPI LISSDLQTAI SNADSSYKIA TSSLTPVFHF
160 170 180 190 200
LNLEKIGTST AIEQDIDFPT LEIANEETKV ALSEATDSLT NFELVKGKES
210 220 230 240 250
ITTVIVNLSP YDAEFSSVLP SNVGLIKIRV YRPWNFSKFL EILPSSVTKI
260 270 280 290 300
AVLQGVSKKS QSNEFQPFLL DFFGNFNELV SRNIEQVVLT NIGNVNDYGN
310 320 330 340 350
VINTVISNIN KKEPDNNLFL GESNEKAEEQ AEVTQLISSV KKVVNLEDAY
360 370 380 390 400
IKVLKQLFSS NLQILNQFSS ETIEPSNPEF GFGRFLKQEA QREELISLAK
410 420 430 440 450
TSLDPSLYLS EDANKIVQLL SKWLSFNGRD LDEAQLQEAN ATGLEIFQLL
460 470 480 490 500
QSNQDSSTVL KFLKIAPTSD SFIFKSSWLI GSDAWSYDLG HSGIQQVLSS
510 520 530 540 550
RKNINVLLID SEPYDHRKQN QDRKKDVGLY AMNYYSAYVA SVAVYASYTQ
560 570 580 590 600
LLTAIIEASK YNGPSIVLAY LPYNSENDTP LEVLKETKNA VESGYWPLYR
610 620 630 640 650
FNPVYDDPST DKEAFSLDSS VIRKQLQDFL DRENKLTLLT RKDPSLSRNL
660 670 680 690 700
KQSAGDALTR KQEKRSKAAF DQLLEGLSGP PLHVYYASDG GNAANLAKRL
710 720 730 740 750
AARASARGLK ATVLSMDDII LEELPGEENV VFITSTAGQG EFPQDGKSFW
760 770 780 790 800
EALKNDTDLD LASLNVAVFG LGDSEYWPRK EDKHYFNKPS QDLFKRLELL
810 820 830 840 850
SAKALIPLGL GDDQDADGFQ TAYSEWEPKL WEALGVSGAA VDDEPKPVTN
860 870 880 890 900
EDIKRESNFL RGTISENLKD TSSGGVTHAN EQLMKFHGIY TQDDRDIREI
910 920 930 940 950
RKSQGLEPYY MFMARARLPG GKTTPQQWLA LDHLSDTSGN GTLKLTTRAT
960 970 980 990 1000
FQIHGVLKKN LKHTLRGMNA VLMDTLAAAG DVNRNVMVSA LPTNAKVHQQ
1010 1020 1030 1040 1050
IADMGKLISD HFLPKTTAYH EVWLEGPEEQ DDDPSWPSIF ENRKDGPRKK
1060 1070 1080 1090 1100
KTLVSGNALV DIEPIYGPTY LPRKFKFNIA VPPYNDVDVL SIDVGLVAIV
1110 1120 1130 1140 1150
NPETQIVEGY NVFVGGGMGT THNNKKTYPR LGSCLGFVKT EDIIPPLEGI
1160 1170 1180 1190 1200
VIVQRDHGDR KDRKHARLKY TVDDMGVEGF KQKVEEYWGK KFEPERPFEF
1210 1220 1230 1240 1250
KSNIDYFGWI KDETGLNHFT AFIENGRVED TPDLPQKTGI RKVAEYMLKT
1260 1270 1280 1290 1300
NSGHFRLTGN QHLVISNITD EHVAGIKSIL KTYKLDNTDF SGLRLSSSSC
1310 1320 1330 1340 1350
VGLPTCGLAF AESERFLPDI ITQLEDCLEE YGLRHDSIIM RMTGCPNGCS
1360 1370 1380 1390 1400
RPWLGELALV GKAPHTYNLM LGGGYLGQRL NKLYKANVKD EEIVDYIKPL
1410 1420 1430 1440
FKRYALEREE GEHFGDFCIR VGIIKPTTEG KYFHEDVSED AY
Length:1,442
Mass (Da):161,219
Last modified:February 1, 1996 - v1
Checksum:iE34695088BA9FE94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49637 Genomic DNA. Translation: CAA89669.1.
BK006943 Genomic DNA. Translation: DAA08922.1.
PIRiS57160.
RefSeqiNP_116579.1. NM_001181795.1.

Genome annotation databases

EnsemblFungiiYJR137C; YJR137C; YJR137C.
GeneIDi853602.
KEGGisce:YJR137C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49637 Genomic DNA. Translation: CAA89669.1.
BK006943 Genomic DNA. Translation: DAA08922.1.
PIRiS57160.
RefSeqiNP_116579.1. NM_001181795.1.

3D structure databases

ProteinModelPortaliP47169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33893. 42 interactions.
IntActiP47169. 8 interactions.
MINTiMINT-4492135.

PTM databases

iPTMnetiP47169.

Proteomic databases

MaxQBiP47169.
PeptideAtlasiP47169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR137C; YJR137C; YJR137C.
GeneIDi853602.
KEGGisce:YJR137C.

Organism-specific databases

EuPathDBiFungiDB:YJR137C.
SGDiS000003898. MET5.

Phylogenomic databases

HOGENOMiHOG000167149.
InParanoidiP47169.
KOiK00381.
OMAiSTTAYHE.
OrthoDBiEOG7DVDK9.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00207.
BioCyciYEAST:MONOMER3O-22.

Miscellaneous databases

PROiP47169.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
3.90.480.10. 2 hits.
InterProiIPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
PR00397. SIROHAEM.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
SSF55124. SSF55124. 2 hits.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
PS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    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., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics."
    Kobayashi K., Yoshimoto A.
    Biochim. Biophys. Acta 705:348-356(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
    Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
    Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
    Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., 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.
    Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMET5_YEAST
AccessioniPrimary (citable) accession number: P47169
Secondary accession number(s): D6VWV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.