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Protein

Sulfite reductase [NADPH] flavoprotein alpha-component

Gene

cysJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • FMNBy similarityNote: Binds 1 FMN 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 alpha-component (cysJ), Sulfite reductase [NADPH] hemoprotein beta-component (cysI)
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)DescriptionActionsGraphical viewLength
Binding sitei495NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi74 – 78FMNPROSITE-ProRule annotation5
Nucleotide bindingi121 – 126FMNPROSITE-ProRule annotation6
Nucleotide bindingi154 – 185FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi392 – 395FADBy similarity4
Nucleotide bindingi525 – 533NADPBy similarity9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis, Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciBSUB:BSU33440-MONOMER.
UniPathwayiUPA00140; UER00207.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] flavoprotein alpha-component (EC:1.8.1.2)
Short name:
SiR-FP
Gene namesi
Name:cysJ
Synonyms:yvgR
Ordered Locus Names:BSU33440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking the cysIJ genes are unable to use sulfate, sulfite or butanesulfonate as sole sulfur source, grow poorly with sulfide, but can still grow with thiosulfate, cysteine or methionine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003884691 – 605Sulfite reductase [NADPH] flavoprotein alpha-componentAdd BLAST605

Proteomic databases

PaxDbiO32214.
PRIDEiO32214.

Expressioni

Inductioni

Up-regulated by sulfate and the transcriptional regulator CysL.2 Publications

Interactioni

Subunit structurei

Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018156.

Structurei

3D structure databases

ProteinModelPortaliO32214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 206Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139
Domaini235 – 454FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST220

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107EER. Bacteria.
COG0369. LUCA.
HOGENOMiHOG000282025.
InParanoidiO32214.
KOiK00380.
OMAiVWYENDP.
PhylomeDBiO32214.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
TIGRFAMsiTIGR01931. cysJ. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLQVMNSPF NQEQAELLNR LLPTLTESQK IWLSGYLSAQ SVSAQEAAGT
60 70 80 90 100
PAAAVSAEAP APAVSKEVTV LYGSQTGNAQ GLAENAGKQL EQSGFQVTVS
110 120 130 140 150
SMSDFKPNQL KKVTNLLIVV STHGEGEPPD NALSFHEFLH GRRAPKLEDL
160 170 180 190 200
RFSVLALGDS SYEFFCQTGK EFDQRLEELG GKRISPRVDC DLDYDEPAAE
210 220 230 240 250
WLEGVLKGLN EAGGGSAAPA PAAASQTGES SYSRTNPFRA EVLENLNLNG
260 270 280 290 300
RGSNKETRHV ELSLEGSGLT YEPGDSLGVY PENDPELVEL LLKEMNWDPE
310 320 330 340 350
EIVTLNKQGD VRPLKEALIS HYEITVLTKP LLEQAAQLTG NDELRELLAP
360 370 380 390 400
GNEENVKAYI EGRDLLDLVR DYGPFSVSAQ EFVSILRKMP ARLYSIASSL
410 420 430 440 450
SANPDEVHLT IGAVRYDAHG RERKGVCSIL CAERLQPGDT LPVYVQHNQN
460 470 480 490 500
FKLPKDPETP IIMVGPGTGV APFRSFMQER EETGAEGKAW MFFGDQHFVT
510 520 530 540 550
DFLYQTEWQN WLKDGVLTKM DVAFSRDTEE KVYVQHRMLE HSAELFEWLQ
560 570 580 590 600
EGAAVYICGD EKHMAHDVHN TLLEIIEKEG NMSREEAEAY LADMQQQKRY

QRDVY
Length:605
Mass (Da):67,259
Last modified:January 1, 1998 - v1
Checksum:i486F512C0AED6217
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15349.1.
PIRiG70040.
RefSeqiNP_391224.1. NC_000964.3.
WP_003243259.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15349; CAB15349; BSU33440.
GeneIDi936022.
KEGGibsu:BSU33440.
PATRICi18978688. VBIBacSub10457_3507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15349.1.
PIRiG70040.
RefSeqiNP_391224.1. NC_000964.3.
WP_003243259.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO32214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018156.

Proteomic databases

PaxDbiO32214.
PRIDEiO32214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15349; CAB15349; BSU33440.
GeneIDi936022.
KEGGibsu:BSU33440.
PATRICi18978688. VBIBacSub10457_3507.

Phylogenomic databases

eggNOGiENOG4107EER. Bacteria.
COG0369. LUCA.
HOGENOMiHOG000282025.
InParanoidiO32214.
KOiK00380.
OMAiVWYENDP.
PhylomeDBiO32214.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00207.
BioCyciBSUB:BSU33440-MONOMER.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
TIGRFAMsiTIGR01931. cysJ. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYSJ_BACSU
AccessioniPrimary (citable) accession number: O32214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.