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Protein

Sulfite reductase [NADPH] flavoprotein alpha-component

Gene

cysJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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.UniRule annotation

Catalytic activityi

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation1 PublicationNote: Binds 1 FAD per subunit.UniRule annotation1 Publication
  • FMNUniRule annotation1 PublicationNote: Binds 1 FMN per subunit.UniRule annotation1 Publication

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 sitei322FADUniRule annotation1 Publication1
Binding sitei356FAD; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei410FADUniRule annotation1 Publication1
Binding sitei561NADPUniRule annotation1 Publication1
Binding sitei599FADUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi70 – 75FMNUniRule annotation1 Publication6
Nucleotide bindingi117 – 120FMNUniRule annotation1 Publication4
Nucleotide bindingi153 – 162FMNUniRule annotation1 Publication10
Nucleotide bindingi386 – 389FADUniRule annotation1 Publication4
Nucleotide bindingi404 – 406FADUniRule annotation1 Publication3
Nucleotide bindingi419 – 422FADUniRule annotation1 Publication4
Nucleotide bindingi519 – 520NADPUniRule annotation1 Publication2
Nucleotide bindingi525 – 529NADPUniRule annotation1 Publication5

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • FMN binding Source: EcoCyc
  • riboflavin reductase (NADPH) activity Source: EcoCyc
  • sulfite reductase (NADPH) activity Source: UniProtKB-HAMAP

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

BioCyciEcoCyc:ALPHACOMP-MONOMER.
ECOL316407:JW2734-MONOMER.
MetaCyc:ALPHACOMP-MONOMER.
BRENDAi1.8.1.2. 2026.
UniPathwayiUPA00140; UER00207.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] flavoprotein alpha-componentUniRule annotation (EC:1.8.1.2UniRule annotation1 Publication)
Short name:
SiR-FPUniRule annotation
Gene namesi
Name:cysJUniRule annotation
Ordered Locus Names:b2764, JW2734
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10191. cysJ.

Subcellular locationi

GO - Cellular componenti

  • sulfite reductase complex (NADPH) Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001999232 – 599Sulfite reductase [NADPH] flavoprotein alpha-componentAdd BLAST598

Proteomic databases

PaxDbiP38038.
PRIDEiP38038.

Interactioni

Subunit structurei

Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ycbXP758634EBI-544440,EBI-544422

Protein-protein interaction databases

BioGridi4262283. 213 interactors.
DIPiDIP-9381N.
IntActiP38038. 3 interactors.
MINTiMINT-1239442.
STRINGi511145.b2764.

Structurei

Secondary structure

1599
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi65 – 69Combined sources5
Beta strandi71 – 73Combined sources3
Helixi74 – 89Combined sources16
Beta strandi94 – 97Combined sources4
Helixi98 – 100Combined sources3
Helixi103 – 108Combined sources6
Beta strandi110 – 117Combined sources8
Helixi120 – 122Combined sources3
Helixi126 – 128Combined sources3
Helixi129 – 135Combined sources7
Beta strandi147 – 153Combined sources7
Beta strandi158 – 160Combined sources3
Helixi163 – 175Combined sources13
Beta strandi178 – 181Combined sources4
Beta strandi184 – 186Combined sources3
Helixi191 – 206Combined sources16
Beta strandi233 – 235Combined sources3
Beta strandi237 – 246Combined sources10
Beta strandi253 – 262Combined sources10
Beta strandi275 – 278Combined sources4
Helixi284 – 293Combined sources10
Beta strandi300 – 304Combined sources5
Beta strandi307 – 310Combined sources4
Helixi311 – 318Combined sources8
Helixi326 – 336Combined sources11
Turni339 – 341Combined sources3
Helixi342 – 344Combined sources3
Helixi349 – 357Combined sources9
Helixi360 – 366Combined sources7
Helixi373 – 379Combined sources7
Beta strandi386 – 390Combined sources5
Turni394 – 396Combined sources3
Beta strandi399 – 407Combined sources9
Beta strandi409 – 412Combined sources4
Beta strandi415 – 418Combined sources4
Helixi420 – 427Combined sources8
Beta strandi434 – 440Combined sources7
Beta strandi455 – 458Combined sources4
Helixi461 – 464Combined sources4
Helixi465 – 477Combined sources13
Beta strandi483 – 490Combined sources8
Helixi492 – 495Combined sources4
Helixi499 – 507Combined sources9
Beta strandi513 – 518Combined sources6
Beta strandi521 – 524Combined sources4
Helixi528 – 534Combined sources7
Helixi536 – 544Combined sources9
Beta strandi548 – 554Combined sources7
Turni555 – 557Combined sources3
Helixi558 – 572Combined sources15
Turni573 – 575Combined sources3
Helixi578 – 590Combined sources13
Beta strandi594 – 599Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DDGX-ray2.01A/B226-599[»]
1DDIX-ray2.51A226-599[»]
1YKGNMR-A53-219[»]
DisProtiDP00190.
ProteinModelPortaliP38038.
SMRiP38038.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38038.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 202Flavodoxin-likeUniRule annotationAdd BLAST139
Domaini234 – 448FAD-binding FR-typeUniRule annotationAdd BLAST215

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.
InParanoidiP38038.
KOiK00380.
OMAiVWYENDP.
PhylomeDBiP38038.

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.

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

P38038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA
60 70 80 90 100
LAATPAPAAE MPGITIISAS QTGNARRVAE ALRDDLLAAK LNVKLVNAGD
110 120 130 140 150
YKFKQIASEK LLIVVTSTQG EGEPPEEAVA LHKFLFSKKA PKLENTAFAV
160 170 180 190 200
FSLGDSSYEF FCQSGKDFDS KLAELGGERL LDRVDADVEY QAAASEWRAR
210 220 230 240 250
VVDALKSRAP VAAPSQSVAT GAVNEIHTSP YSKDAPLVAS LSVNQKITGR
260 270 280 290 300
NSEKDVRHIE IDLGDSGMRY QPGDALGVWY QNDPALVKEL VELLWLKGDE
310 320 330 340 350
PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK
360 370 380 390 400
LQHYAATTPI VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQAEVENE
410 420 430 440 450
VHVTVGVVRY DVEGRARAGG ASSFLADRVE EEGEVRVFIE HNDNFRLPAN
460 470 480 490 500
PETPVIMIGP GTGIAPFRAF MQQRAADEAP GKNWLFFGNP HFTEDFLYQV
510 520 530 540 550
EWQRYVKDGV LTRIDLAWSR DQKEKVYVQD KLREQGAELW RWINDGAHIY
560 570 580 590
VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY
Length:599
Mass (Da):66,270
Last modified:January 23, 2007 - v4
Checksum:i6B39EF5C25265113
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156S → T in AAA23650 (PubMed:2550423).Curated1
Sequence conflicti268M → L in AAA23650 (PubMed:2550423).Curated1
Sequence conflicti508D → E in AAA23650 (PubMed:2550423).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23008 Genomic DNA. Translation: AAA23650.1.
U29579 Genomic DNA. Translation: AAA69274.1.
U00096 Genomic DNA. Translation: AAC75806.1.
AP009048 Genomic DNA. Translation: BAE76841.1.
PIRiH65057.
RefSeqiNP_417244.1. NC_000913.3.
WP_000211913.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75806; AAC75806; b2764.
BAE76841; BAE76841; BAE76841.
GeneIDi947239.
KEGGiecj:JW2734.
eco:b2764.
PATRICi32120940. VBIEscCol129921_2862.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23008 Genomic DNA. Translation: AAA23650.1.
U29579 Genomic DNA. Translation: AAA69274.1.
U00096 Genomic DNA. Translation: AAC75806.1.
AP009048 Genomic DNA. Translation: BAE76841.1.
PIRiH65057.
RefSeqiNP_417244.1. NC_000913.3.
WP_000211913.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DDGX-ray2.01A/B226-599[»]
1DDIX-ray2.51A226-599[»]
1YKGNMR-A53-219[»]
DisProtiDP00190.
ProteinModelPortaliP38038.
SMRiP38038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262283. 213 interactors.
DIPiDIP-9381N.
IntActiP38038. 3 interactors.
MINTiMINT-1239442.
STRINGi511145.b2764.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP38038.
PRIDEiP38038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75806; AAC75806; b2764.
BAE76841; BAE76841; BAE76841.
GeneIDi947239.
KEGGiecj:JW2734.
eco:b2764.
PATRICi32120940. VBIEscCol129921_2862.

Organism-specific databases

EchoBASEiEB0188.
EcoGeneiEG10191. cysJ.

Phylogenomic databases

eggNOGiENOG4107EER. Bacteria.
COG0369. LUCA.
HOGENOMiHOG000282025.
InParanoidiP38038.
KOiK00380.
OMAiVWYENDP.
PhylomeDBiP38038.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00207.
BioCyciEcoCyc:ALPHACOMP-MONOMER.
ECOL316407:JW2734-MONOMER.
MetaCyc:ALPHACOMP-MONOMER.
BRENDAi1.8.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP38038.
PROiP38038.

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_ECOLI
AccessioniPrimary (citable) accession number: P38038
Secondary accession number(s): P14782, Q2MA65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 156 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.