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Protein

Assimilatory sulfite reductase (ferredoxin), chloroplastic

Gene

SIR

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth.1 Publication
DNA-binding protein that binds to both double-stranded and single-stranded DNA without significant sequence specificity to reversibly repress the transcriptional activity of chloroplast nucleoids by promoting DNA compaction and possibly regulate DNA replication.By similarity

Catalytic activityi

Hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+.1 Publication

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi503 – 5031Iron-sulfur (4Fe-4S)By similarity
Metal bindingi509 – 5091Iron-sulfur (4Fe-4S)By similarity
Metal bindingi549 – 5491Iron-sulfur (4Fe-4S)By similarity
Metal bindingi553 – 5531Iron (siroheme axial ligand)By similarity
Metal bindingi553 – 5531Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • copper ion binding Source: TAIR
  • DNA binding Source: UniProtKB
  • heme binding Source: InterPro
  • sulfite reductase (ferredoxin) activity Source: UniProtKB
  • sulfite reductase activity Source: TAIR

GO - Biological processi

  • DNA packaging Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • response to cold Source: TAIR
  • response to salt stress Source: TAIR
  • sulfide oxidation, using siroheme sulfite reductase Source: UniProtKB
  • sulfur compound metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:AT5G04590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Assimilatory sulfite reductase (ferredoxin), chloroplastic (EC:1.8.7.11 Publication)
Short name:
AtSiR
Alternative name(s):
Sulfite reductase (ferredoxin)
Gene namesi
Name:SIR
Ordered Locus Names:At5g04590
ORF Names:T32M21.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G04590.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast nucleoid Source: UniProtKB
  • chloroplast stroma Source: TAIR
  • membrane Source: TAIR
  • plastid Source: TAIR
  • stromule Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161ChloroplastSequence analysisAdd
BLAST
Chaini62 – 642581Assimilatory sulfite reductase (ferredoxin), chloroplasticPRO_0000416844Add
BLAST

Post-translational modificationi

Phosphorylated; this phosphorylation reduces DNA-binding.By similarity

Keywords - PTMi

Thioether bond

Proteomic databases

PaxDbiQ9LZ66.
PRIDEiQ9LZ66.

PTM databases

SwissPalmiQ9LZ66.

Expressioni

Tissue specificityi

Present in leaves and roots.1 Publication

Inductioni

Rapidly induced by sulfur dioxide SO2 in a sulfite oxidase (SO)-dependent manner.1 Publication

Gene expression databases

GenevisibleiQ9LZ66. AT.

Interactioni

Subunit structurei

Monomer. Interacts with ferredoxin (By similarity).By similarity

Protein-protein interaction databases

BioGridi15615. 1 interaction.
STRINGi3702.AT5G04590.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LZ66.
SMRiQ9LZ66. Positions 132-626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0560. Eukaryota.
COG0155. LUCA.
HOGENOMiHOG000218417.
InParanoidiQ9LZ66.
KOiK00392.
OMAiMGMTHGD.
PhylomeDBiQ9LZ66.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR011787. SiR_ferredoxin-dep.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
TIGRFAMsiTIGR02042. sir. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LZ66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTFRAPAG AATVFTADQK IRLGRLDALR SSHSVFLGRY GRGGVPVPPS
60 70 80 90 100
ASSSSSSPIQ AVSTPAKPET ATKRSKVEII KEKSNFIRYP LNEELLTEAP
110 120 130 140 150
NVNESAVQLI KFHGSYQQYN REERGGRSYS FMLRTKNPSG KVPNQLYLTM
160 170 180 190 200
DDLADEFGIG TLRLTTRQTF QLHGVLKQNL KTVMSSIIKN MGSTLGACGD
210 220 230 240 250
LNRNVLAPAA PYVKKDYLFA QETADNIAAL LSPQSGFYYD MWVDGEQFMT
260 270 280 290 300
AEPPEVVKAR NDNSHGTNFV DSPEPIYGTQ FLPRKFKVAV TVPTDNSVDL
310 320 330 340 350
LTNDIGVVVV SDENGEPQGF NIYVGGGMGR THRMESTFAR LAEPIGYVPK
360 370 380 390 400
EDILYAVKAI VVTQREHGRR DDRKYSRMKY LISSWGIEKF RDVVEQYYGK
410 420 430 440 450
KFEPSRELPE WEFKSYLGWH EQGDGAWFCG LHVDSGRVGG IMKKTLREVI
460 470 480 490 500
EKYKIDVRIT PNQNIVLCDI KTEWKRPITT VLAQAGLLQP EFVDPLNQTA
510 520 530 540 550
MACPAFPLCP LAITEAERGI PSILKRVRAM FEKVGLDYDE SVVIRVTGCP
560 570 580 590 600
NGCARPYMAE LGLVGDGPNS YQVWLGGTPN LTQIARSFMD KVKVHDLEKV
610 620 630 640
CEPLFYHWKL ERQTKESFGE YTTRMGFEKL KELIDTYKGV SQ
Length:642
Mass (Da):71,950
Last modified:October 1, 2000 - v1
Checksum:iA00E4F12C278CFA3
GO

Sequence cautioni

The sequence AAK82552.1 differs from that shown. Reason: Erroneous termination at position 417. Translated as Leu.Curated
The sequence AAN18162.1 differs from that shown. Reason: Erroneous termination at position 417. Translated as Leu.Curated
The sequence CAA71239.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031R → K in AAK82552 (PubMed:14593172).Curated
Sequence conflicti203 – 2031R → K in AAN18162 (PubMed:14593172).Curated
Sequence conflicti426 – 4261A → T in CAA89154 (PubMed:8695637).Curated
Sequence conflicti554 – 5541A → R in CAA71239 (PubMed:9661674).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49217 mRNA. Translation: CAA89154.1.
Y10157 Genomic DNA. Translation: CAA71239.1. Sequence problems.
AL162875 Genomic DNA. Translation: CAB85565.1.
CP002688 Genomic DNA. Translation: AED90762.1.
AF325027 mRNA. Translation: AAG40379.1.
AY048290 mRNA. Translation: AAK82552.1. Sequence problems.
BT000593 mRNA. Translation: AAN18162.1. Sequence problems.
AK229873 mRNA. Translation: BAF01702.1.
PIRiS71437.
T48455.
RefSeqiNP_196079.1. NM_120541.3.
UniGeneiAt.25240.

Genome annotation databases

EnsemblPlantsiAT5G04590.1; AT5G04590.1; AT5G04590.
GeneIDi830336.
GrameneiAT5G04590.1; AT5G04590.1; AT5G04590.
KEGGiath:AT5G04590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49217 mRNA. Translation: CAA89154.1.
Y10157 Genomic DNA. Translation: CAA71239.1. Sequence problems.
AL162875 Genomic DNA. Translation: CAB85565.1.
CP002688 Genomic DNA. Translation: AED90762.1.
AF325027 mRNA. Translation: AAG40379.1.
AY048290 mRNA. Translation: AAK82552.1. Sequence problems.
BT000593 mRNA. Translation: AAN18162.1. Sequence problems.
AK229873 mRNA. Translation: BAF01702.1.
PIRiS71437.
T48455.
RefSeqiNP_196079.1. NM_120541.3.
UniGeneiAt.25240.

3D structure databases

ProteinModelPortaliQ9LZ66.
SMRiQ9LZ66. Positions 132-626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15615. 1 interaction.
STRINGi3702.AT5G04590.1.

PTM databases

SwissPalmiQ9LZ66.

Proteomic databases

PaxDbiQ9LZ66.
PRIDEiQ9LZ66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G04590.1; AT5G04590.1; AT5G04590.
GeneIDi830336.
GrameneiAT5G04590.1; AT5G04590.1; AT5G04590.
KEGGiath:AT5G04590.

Organism-specific databases

TAIRiAT5G04590.

Phylogenomic databases

eggNOGiKOG0560. Eukaryota.
COG0155. LUCA.
HOGENOMiHOG000218417.
InParanoidiQ9LZ66.
KOiK00392.
OMAiMGMTHGD.
PhylomeDBiQ9LZ66.

Enzyme and pathway databases

BioCyciMetaCyc:AT5G04590-MONOMER.

Miscellaneous databases

PROiQ9LZ66.

Gene expression databases

GenevisibleiQ9LZ66. AT.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR011787. SiR_ferredoxin-dep.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
TIGRFAMsiTIGR02042. sir. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase."
    Bruehl A., Haverkamp T., Gisselmann G., Schwenn J.D.
    Biochim. Biophys. Acta 1295:119-124(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
    Tissue: Leaf.
  2. "Isolation and characterization of a gene for assimilatory sulfite reductase from Arabidopsis thaliana."
    Bork C., Schwenn J.D., Hell R.
    Gene 212:147-153(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-642.
    Strain: cv. Columbia.
  7. "Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
    Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
    J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
    Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
    Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. "The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature."
    Goulas E., Schubert M., Kieselbach T., Kleczkowski L.A., Gardestroem P., Schroeder W., Hurry V.
    Plant J. 47:720-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. "Sulfite oxidase protects plants against sulfur dioxide toxicity."
    Brychkova G., Xia Z., Yang G., Yesbergenova Z., Zhang Z., Davydov O., Fluhr R., Sagi M.
    Plant J. 50:696-709(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SULFUR DIOXIDE.
  11. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
    Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
    PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
    Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
    Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. "Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
    Olinares P.D., Ponnala L., van Wijk K.J.
    Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  14. "Sulfite reductase defines a newly discovered bottleneck for assimilatory sulfate reduction and is essential for growth and development in Arabidopsis thaliana."
    Khan M.S., Haas F.H., Samami A.A., Gholami A.M., Bauer A., Fellenberg K., Reichelt M., Haensch R., Mendel R.R., Meyer A.J., Wirtz M., Hell R.
    Plant Cell 22:1216-1231(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiSIR_ARATH
AccessioniPrimary (citable) accession number: Q9LZ66
Secondary accession number(s): O23650
, Q0WMF4, Q42590, Q94AB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.