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Protein

Sulfite reductase [NADPH] flavoprotein alpha-component

Gene

cysJ

Organism
Shewanella oneidensis (strain MR-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation
  • FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes hydrogen sulfide from sulfite (NADPH route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Sulfite reductase [NADPH] hemoprotein beta-component (cysI), Sulfite reductase [NADPH] flavoprotein alpha-component (cysJ)
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 sitei327FADUniRule annotation1
Binding sitei361FAD; via carbonyl oxygenUniRule annotation1
Binding sitei569NADPUniRule annotation1
Binding sitei607FADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi72 – 77FMNUniRule annotation6
Nucleotide bindingi119 – 122FMNUniRule annotation4
Nucleotide bindingi155 – 164FMNUniRule annotation10
Nucleotide bindingi395 – 398FADUniRule annotation4
Nucleotide bindingi413 – 415FADUniRule annotation3
Nucleotide bindingi428 – 431FADUniRule annotation4
Nucleotide bindingi527 – 528NADPUniRule annotation2
Nucleotide bindingi533 – 537NADPUniRule annotation5

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • FMN binding Source: InterPro
  • sulfite reductase (NADPH) activity Source: TIGR

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

UniPathwayiUPA00140; UER00207.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] flavoprotein alpha-componentUniRule annotation (EC:1.8.1.2UniRule annotation)
Short name:
SiR-FPUniRule annotation
Gene namesi
Name:cysJUniRule annotation
Ordered Locus Names:SO_3738
OrganismiShewanella oneidensis (strain MR-1)
Taxonomic identifieri211586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000008186 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001999361 – 607Sulfite reductase [NADPH] flavoprotein alpha-componentAdd BLAST607

Proteomic databases

PaxDbiQ8EAZ9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi211586.SO_3738.

Structurei

3D structure databases

ProteinModelPortaliQ8EAZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 204Flavodoxin-likeUniRule annotationAdd BLAST139
Domaini239 – 456FAD-binding FR-typeUniRule annotationAdd BLAST218

Sequence similaritiesi

Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family.UniRule annotation
In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation
Contains 1 flavodoxin-like domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107EER. Bacteria.
COG0369. LUCA.
HOGENOMiHOG000282025.
KOiK00380.
OMAiVWYENDP.
OrthoDBiPOG091H04ZI.
PhylomeDBiQ8EAZ9.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_01541. CysJ. 1 hit.
InterProiIPR010199. CysJ.
IPR029758. CysJ_Proteobact.
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.

Q8EAZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLKELSSLA SPLSQSQVDK LKQLTAELNS VQLAWVSGYL AATANTSGSA
60 70 80 90 100
IQVAASVTEA QAAQTVTILY GSQTGNGRGI AKALAEKAKT QGYSVNLASM
110 120 130 140 150
GEYNVRQLKQ ETLLLLVVST HGEGEAPDDA IELHKFLATK RAPQLNNLHY
160 170 180 190 200
SVLALGDSSY EFFCQTGKDF DARLSALGAK ALLPLVECDV DYEAAAGQWH
210 220 230 240 250
ADVLTAVKPL IQTTANVVAL NEINSTSAQV ASESEFTKQN PYRAEVLVSQ
260 270 280 290 300
KITGRDSDRD VRHVEIDLGE SGLHYEVGDA LGVWFSNSEI LVGEILAGLG
310 320 330 340 350
LAADAKVTVG SESISLKQAL IDKKELTQLY PGLVKAWAEL SASSELLALS
360 370 380 390 400
EDKEQLRQFI LNHQFVDLVT NYKLPAEANL DANKLLELLR PLTPRLYSIA
410 420 430 440 450
SSQTEVDTEV HLTVALVEDE HQGQTRFGGA SHFLASAQEG AEVKVYVEPN
460 470 480 490 500
KHFRLPENPD TPVIMIGPGT GVAPFRAFMQ ERVAQGAKGD SWLFFGNPHF
510 520 530 540 550
EQDFLYQTEW QQYLKNGDLT RIDVAFSRDQ AHKIYVQHRI KEQGQALWQW
560 570 580 590 600
LQNGAHLYIC GDAERMAKDV HQALLAVAVE FGGLSSEAAE EYFETLRSHK

RYQKDVY
Length:607
Mass (Da):66,620
Last modified:March 1, 2003 - v1
Checksum:iC6042663547ACD22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN56721.1.
RefSeqiNP_719277.1. NC_004347.2.
WP_011073521.1. NC_004347.2.

Genome annotation databases

EnsemblBacteriaiAAN56721; AAN56721; SO_3738.
GeneIDi1171388.
KEGGison:SO_3738.
PATRICi23527152. VBISheOne101494_3621.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN56721.1.
RefSeqiNP_719277.1. NC_004347.2.
WP_011073521.1. NC_004347.2.

3D structure databases

ProteinModelPortaliQ8EAZ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211586.SO_3738.

Proteomic databases

PaxDbiQ8EAZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN56721; AAN56721; SO_3738.
GeneIDi1171388.
KEGGison:SO_3738.
PATRICi23527152. VBISheOne101494_3621.

Phylogenomic databases

eggNOGiENOG4107EER. Bacteria.
COG0369. LUCA.
HOGENOMiHOG000282025.
KOiK00380.
OMAiVWYENDP.
OrthoDBiPOG091H04ZI.
PhylomeDBiQ8EAZ9.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00207.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_01541. CysJ. 1 hit.
InterProiIPR010199. CysJ.
IPR029758. CysJ_Proteobact.
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_SHEON
AccessioniPrimary (citable) accession number: Q8EAZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2003
Last modified: October 5, 2016
This is version 86 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.