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A1KU05 (CYSI_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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] hemoprotein beta-component

Short name=SiR-HP
Short name=SiRHP
EC=1.8.1.2
Gene names
Name:cysI
Ordered Locus Names:NMC1091
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length589 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 By similarity. HAMAP MF_01540

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540

Cofactor

Binds 1 siroheme per subunit By similarity. HAMAP MF_01540

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01540

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP MF_01540

Subunit structure

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

Sequence similarities

Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540
PRO_1000068766

Sites

Metal binding4431Iron-sulfur (4Fe-4S) By similarity
Metal binding4491Iron-sulfur (4Fe-4S) By similarity
Metal binding4881Iron-sulfur (4Fe-4S) By similarity
Metal binding4921Iron (siroheme axial ligand) By similarity
Metal binding4921Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KU05 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 8659C0997E0CE46B

FASTA58965,964
        10         20         30         40         50         60 
MTVQTKTKGL AWQEKPLSDN ERLKTESNFL RGTILDDLKD PLTGGFKGDN FQLIRFHGMY 

        70         80         90        100        110        120 
EQDDRDIRAE RAEAKLEPLK FMLLRCRLPG GIIKPSQWIE LDKFARENSH YRSIRLTNRQ 

       130        140        150        160        170        180 
TFQFHGVPKA KLQTMHRLLH KLGLDSIATA ADMNRNVLCT SNPIESELHR QAYEYAKKIS 

       190        200        210        220        230        240 
EHLLPRTRGY LDVWVDGKKV QSSDDFLQED EPILGKTYLP RKFKTAVVIP PLNDVDCYGN 

       250        260        270        280        290        300 
DLDFVAVSDG NGQLAGFNVL AGGGLSMEHG NTKTYPNISL ELGFVPPEHA LKAAEAVVTT 

       310        320        330        340        350        360 
QRDFGNRSDR KNARTRYTIQ NMGLDNFRAE VERRMGMPFE PIRPFKFTGR GDRIGWVKGI 

       370        380        390        400        410        420 
DGNWHLTLFI ESGRLVDEGG KQLLTGVLEI AKIHKGDFRI TANQNLIVAN VAEADKAKIE 

       430        440        450        460        470        480 
ELARTYGLIR NDVSKLRENA MSCVSFPTCP LAMAEAERVL PDFIGELDKI MAKHGTSDDY 

       490        500        510        520        530        540 
IVTRITGCPN GCGRAMLAEI GLVGKAVGRY NLHIGGDREG VRIPRLYKEN ITLPEILSEL 

       550        560        570        580 
DDLIGKWAAG RDTDEGFGDF AIRTGIVKPV LDAPVDFWDA SKAVPIARA 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed: 17305430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM10346.1.
RefSeqYP_975134.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KU05.
SMRA1KU05. Positions 83-579.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1KU05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000007545; EBNEIP00000007314; EBNEIG00000007545.
GeneID4676437.
GenomeReviewsGene locus NMC1091 in contig AM421808_GR.
KEGGnmc:NMC1091.
NMPDRfig|487.2.peg.2214.
PATRIC20352149. VBINeiMen17609_1327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0155.
GeneTreeEBGT00050000021777.
HOGENOMHBG626671.
OMAMTLDGFR.
PhylomeDBA1KU05.
ProtClustDBPRK13504.

Enzyme and pathway databases

BioCycNMEN272831:NMC1091-MONOMER.

Family and domain databases

HAMAPMF_01540. CysI.
[Tree]
InterProIPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
Gene3DG3DSA:3.90.480.10. G3DSA:3.90.480.10. 2 hits.
KOK00381.
PfamPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSPR00397. SIROHAEM.
SUPFAMSSF55124. NiR_SiRalpha_1/3. 2 hits.
TIGRFAMsTIGR02041. CysI. 1 hit.
PROSITEPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSI_NEIMF
AccessionPrimary (citable) accession number: A1KU05
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 41 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