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Protein

Sulfite reductase [NADPH] flavoprotein alpha-component

Gene

cysJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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
  • NADP+ binding Source: CAFA
  • riboflavin reductase (NADPH) activity Source: EcoCyc
  • sulfite reductase (NADPH) activity Source: UniProtKB-EC

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Cysteine biosynthesis, Electron transport, Transport
LigandFAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciEcoCyc:ALPHACOMP-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

Pathology & Biotechi

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB03147 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

Alpha8-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ycbXP758635EBI-544440,EBI-544422

Protein-protein interaction databases

BioGridi4262283, 220 interactors
DIPiDIP-9381N
IntActiP38038, 4 interactors
STRINGi316385.ECDH10B_2932

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

Phylogenomic databases

eggNOGiENOG4107EER Bacteria
COG0369 LUCA
HOGENOMiHOG000282025
InParanoidiP38038
KOiK00380
OMAiTKMDVAF
PhylomeDBiP38038

Family and domain databases

Gene3Di1.20.990.10, 1 hit
3.40.50.360, 1 hit
HAMAPiMF_01541 CysJ, 1 hit
InterProiView protein in InterPro
IPR010199 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_sf
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR001433 OxRdtase_FAD/NAD-bd
IPR017938 Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00667 FAD_binding_1, 1 hit
PF00258 Flavodoxin_1, 1 hit
PF00175 NAD_binding_1, 1 hit
PIRSFiPIRSF000207 SiR-FP_CysJ, 1 hit
PRINTSiPR00369 FLAVODOXIN
PR00371 FPNCR
SUPFAMiSSF52218 SSF52218, 1 hit
SSF63380 SSF63380, 1 hit
TIGRFAMsiTIGR01931 cysJ, 1 hit
PROSITEiView protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit

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
PATRICifig|1411691.4.peg.3973

Similar proteinsi

Entry informationi

Entry nameiCYSJ_ECOLI
AccessioniPrimary (citable) accession number: P38038
Secondary accession number(s): P14782, Q2MA65
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 166 of the entry and version 4 of the sequence. See 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
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Main funding by: National Institutes of Health