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Q9JS45 (CYSJ_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sulfite reductase [NADPH] flavoprotein alpha-component
Short name=SiR-FP
EC=1.8.1.2
Gene names
Name:cysJ1
Synonyms:cysJ-1
Ordered Locus Names:NMB1152
AND
Name:cysJ2
Synonyms:cysJ-2
Ordered Locus Names:NMB1190
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01541

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP-Rule MF_01541

Cofactor

Binds 1 FAD per subunit By similarity.

Binds 1 FMN per subunit By similarity.

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP-Rule MF_01541

Subunit structure

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

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 604604Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP-Rule MF_01541
PRO_0000199929

Regions

Domain66 – 204139Flavodoxin-like
Domain239 – 453215FAD-binding FR-type
Nucleotide binding72 – 765FMN By similarity
Nucleotide binding119 – 1246FMN By similarity
Nucleotide binding152 – 18332FMN By similarity
Nucleotide binding391 – 3944FAD By similarity
Nucleotide binding425 – 4273FAD By similarity
Nucleotide binding524 – 5329NADP By similarity

Sites

Binding site4941NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JS45 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 33BDC8B846E56264

FASTA60466,386
        10         20         30         40         50         60 
MSEHDMQNTN PPLPPLPPEI TQLLSGLDAA QWAWLSGYAW AKAGNGASAG LPALQTALPA 

        70         80         90        100        110        120 
AEPFSVTVLS ASQTGNAKSV ADKAADSLEA AGIQVSRAEL KDYKAKNIAG ERRLLLVTST 

       130        140        150        160        170        180 
QGEGEPPKEA VVLHKLLNGK KAPKLDKLQF AVLGLGDSSY PNFCQAGKDF DRRFEELGAK 

       190        200        210        220        230        240 
RLLERVDADL DFTASANAWT DNIAALLKEE AAKNRATPAP QTTPPAGLQT APDGRYCKAA 

       250        260        270        280        290        300 
PFPAALLANQ KITARQSDKD VRHIEIDLSG SDLHYLPGDA LGVWFDNDPA LVREILDLLG 

       310        320        330        340        350        360 
IDPATEIQAG GKMMPVARAL SSHFELTQNT PAFVKGYAAF AHYEELDKII ADNAVLQDFV 

       370        380        390        400        410        420 
QNTPIVDVLH RFPASLTAEQ FIRLLRPLAP RLYSISSAQA EVGDEVHLTV GVVRFEHEGR 

       430        440        450        460        470        480 
ARTGGASGFL ADRLEEDGTV RVFVERNDGF RLPEDSRKPI VMIGSGTGVA PFRAFVQQRA 

       490        500        510        520        530        540 
AENAEGKNWL IFGNPHFARD FLYQTEWQQF AKDGFLHRYD FAWSRDQEEK IYVQDKIREQ 

       550        560        570        580        590        600 
AEGLWQWLQE GAHIYVCGDA AKMAKDVEAA LLDVIIGAGH LDEEGAEEYL DMLREEKRYQ 


RDVY

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF41573.1.
AE002098 Genomic DNA. Translation: AAF41538.1.
PIRH81110.
RefSeqNP_274180.1. NC_003112.2.
NP_274216.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9JS45.
SMRQ9JS45. Positions 228-604.
ModBaseSearch...

Protein-protein interaction databases

STRING122586.NMB1190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF41538; AAF41538; NMB1152.
AAF41573; AAF41573; NMB1190.
GeneID903573.
903610.
KEGGnme:NMB1152.
nme:NMB1190.
PATRIC20357883. VBINeiMen85645_1457.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282025.
KOK00380.
OMASDKDVRH.
ProtClustDBCLSK877924.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-1151-MONOMER.
NMEN122586:GHGG-1188-MONOMER.
UniPathwayUPA00140; UER00207.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
HAMAPMF_01541. CysJ.
InterProIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMsTIGR01931. cysJ. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSJ_NEIMB
AccessionPrimary (citable) accession number: Q9JS45
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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