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Q1LTP1 (CYSJ_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:cysJ
Ordered Locus Names:BCI_0218
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length595 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 MF_01541

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP MF_01541

Binds 1 FMN per subunit By similarity. HAMAP MF_01541

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP 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 – 595595Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_0000292965

Regions

Domain59 – 197139Flavodoxin-like
Domain230 – 444215FAD-binding FR-type
Nucleotide binding65 – 695FMN By similarity
Nucleotide binding112 – 1176FMN By similarity
Nucleotide binding145 – 17632FMN By similarity
Nucleotide binding382 – 3854FAD By similarity
Nucleotide binding416 – 4183FAD By similarity
Nucleotide binding515 – 5239NADP By similarity

Sites

Binding site4851NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LTP1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: F6F314B06CE8CAAC

FASTA59567,733
        10         20         30         40         50         60 
MTQQNAPKDL PPLSAEQLDR LQAISSDLSN LQLAWASGYL WNKASHSIPI DYTASQQVIT 

        70         80         90        100        110        120 
VLSASQTGNA RRLAVQLYED LLAAQLSVVI INAGDYKFKQ IAQEKWLLIV TSTQGDGDPP 

       130        140        150        160        170        180 
EEAIALYKYL FSKKAPVLNN IQFAIFGLGD SSYTYFAKIG KDFDSRLAEL GAQRLYDRVD 

       190        200        210        220        230        240 
ADVDYQEKAD IWRREIVKIL QTKLVTVNAK QQLSVINNRI EVKNNLYTKE EPFTAHLVVK 

       250        260        270        280        290        300 
QKITSRSSKK DIRHLEIDIA GSGLNYQPGD ALGVWYENDP VLISEILELL GLTGNELVQV 

       310        320        330        340        350        360 
KEKNIPLNEA LQKHYELTNN TAEIVKSYAY ITRNSSLLAL VDDQQQLKQF AFSTPFIDMI 

       370        380        390        400        410        420 
QRIPVELHPK QLLTLLRPLM PRLYSIASSQ AEVGDEVHLT VSVVRYEIDG KIRTGGASSY 

       430        440        450        460        470        480 
LAYRLQESEP IRVFIEHNDN FRLPNNPNTA IIMIGSGTGI APFRGFMQQR EATTAKGKNW 

       490        500        510        520        530        540 
LFFGNQHLTD DFLYQVEWQR YIKNGLLNKI DVAWSQDQNK KIYVQDRLLE KGIELWNWIQ 

       550        560        570        580        590 
DGAHIYVCGN ANLMARDVEK ALVKLIAIHG RMDYEQADEF LSELRIARRF QRDTY

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000238 Genomic DNA. Translation: ABF14003.1.
RefSeqYP_588673.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTP1.
SMRQ1LTP1. Positions 59-203, 227-595.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTP1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056751.
GenomeReviewsGene locus BCI_0218 in contig CP000238_GR.
KEGGbci:BCI_0218.
PATRIC21073935. VBIBauCic75062_0206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHBG736048.
OMAESADEYL.
PhylomeDBQ1LTP1.
ProtClustDBPRK10953.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0218-MONOMER.

Family and domain databases

HAMAPMF_01541. CysJ.
[Tree]
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]
Gene3DG3DSA:1.20.990.10. NADPH_Cyt_P450_Rdtase_dom3. 1 hit.
KOK00380.
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_BAUCH
AccessionPrimary (citable) accession number: Q1LTP1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 38 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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