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Reviewed, UniProtKB/Swiss-Prot Q3IFM1 (CYSI_PSEHT)

Last modified November 25, 2008. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: PSHAa0155
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

This enzyme 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.

Catalytic activity

H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.

Cofactor

Binds 1 siroheme per subunit By similarity.

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

Subunit structure

Alpha(8)-beta(4). 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 – 565565Sulfite reductase [NADPH] hemoprotein beta-component
PRO_0000292962

Sites

Metal binding4291Iron-sulfur (4Fe-4S) By similarity
Metal binding4351Iron-sulfur (4Fe-4S) By similarity
Metal binding4741Iron-sulfur (4Fe-4S) By similarity
Metal binding4781Iron (siroheme axial ligand) By similarity
Metal binding4781Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IFM1-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: F622A443A6723502

FASTA56562,933
        10         20         30         40         50         60 
MSEQDKNVKL SDNERMKRES NFLRGTIATD LKDEITGGFT ADNFQLIRFH GMYQQDDRDI 

        70         80         90        100        110        120 
RGERAKQKLE PLHNVMLRAR MPGGIIKPEQ WLAIDKFAEE KTSYGSIRLT TRQTFQFHGV 

       130        140        150        160        170        180 
LKPNIKGMHQ LLDSVGIDSI ATAGDVNRNV LCTTNPVESE LHQEAYEWAA KISEHLLPKT 

       190        200        210        220        230        240 
KAYAEIWLNG EKAETTEEPI LGSNYLPRKF KTTVTIPPNN EVDVHANDLN FVAIAENGKL 

       250        260        270        280        290        300 
IGFNVLVGGG LAMTHGDTAT YPRKADDFGF IPLEHTLKIA EHVVSVQRDW GNRSNRKNAK 

       310        320        330        340        350        360 
TKYTLDRVGV DVFKAEVEKR AGVEFASSRP YKFTHRGDRI GWVEGIDGKH HLTLFIQSGR 

       370        380        390        400        410        420 
ILDYPDKPLK TGCRKIAEVH QGDMRMTANQ NLIIAGVAAN QKAVIEEIAR NHGLIDDKDT 

       430        440        450        460        470        480 
EQRKNSMACV ALPTCPLAMA EAERYLPSLV EKIEALLAKH GVPNDSIIMR VVGCPNGCGR 

       490        500        510        520        530        540 
AMLAEAGLVG KGPGKYNVYL GGNLEGTRIP KLYLENVGED VYLAAFDELI GQWVNERNDG 

       550        560 
ECFGDFVIRK GIVAEVKVSV TDFHA 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR954246 Genomic DNA. Translation: CAI85259.1.
RefSeqYP_338702.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3709416.
GenomeReviewsGene locus PSHAa0155 in contig CR954246_GR.
KEGGpha:PSHAa0155.
NMPDRfig|326442.4.peg.240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3IFM1.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA0155-MON.

Family and domain databases

HAMAPMF_01540.
[Tree]
InterProIPR011786. CysI.
IPR006066. Nir_Si_BS.
IPR006067. Nir_Sir_4Fe4S.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
[Graphical view]
PfamPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSPR00397. SIROHAEM.
TIGRFAMsTIGR02041. CysI. 1 hit.
PROSITEPS00365. NIR_SIR. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSI_PSEHT
AccessionPrimary (citable) accession number: Q3IFM1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: November 8, 2005
Last modified: November 25, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents