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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: 3 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei497 – 4971NADPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 765FMNUniRule annotation
Nucleotide bindingi119 – 1246FMNUniRule annotation
Nucleotide bindingi152 – 18332FMNUniRule annotationAdd
BLAST
Nucleotide bindingi395 – 3984FADUniRule annotation
Nucleotide bindingi429 – 4313FADUniRule annotation
Nucleotide bindingi527 – 5359NADPUniRule annotation

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. FMN binding Source: InterPro
  3. iron ion binding Source: InterPro
  4. sulfite reductase (NADPH) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cysteine biosynthetic process Source: UniProtKB-KW
  2. hydrogen sulfide biosynthetic process Source: UniProtKB-HAMAP
  3. sulfate assimilation Source: UniProtKB-HAMAP
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
ProteomesiUP000008186 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Sulfite reductase [NADPH] flavoprotein alpha-componentPRO_0000199936Add
BLAST

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.
SMRiQ8EAZ9. Positions 234-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 204139Flavodoxin-likeUniRule annotationAdd
BLAST
Domaini239 – 456218FAD-binding FR-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0369.
HOGENOMiHOG000282025.
KOiK00380.
OMAiGVWYEND.
OrthoDBiEOG6CVV7G.
PhylomeDBiQ8EAZ9.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_01541. CysJ.
InterProiIPR010199. CysJ.
IPR029758. CysJ_Proteobact.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
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:February 28, 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.

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.

3D structure databases

ProteinModelPortaliQ8EAZ9.
SMRiQ8EAZ9. Positions 234-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211586.SO_3738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0369.
HOGENOMiHOG000282025.
KOiK00380.
OMAiGVWYEND.
OrthoDBiEOG6CVV7G.
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.
InterProiIPR010199. CysJ.
IPR029758. CysJ_Proteobact.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MR-1.

Entry informationi

Entry nameiCYSJ_SHEON
AccessioniPrimary (citable) accession number: Q8EAZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 12, 2005
Last sequence update: February 28, 2003
Last modified: January 6, 2015
This is version 77 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

External Data

Dasty 3

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 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.