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A8ANX1 (CYSJ_CITK8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:CKO_04119
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

Protein attributes

Sequence length601 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 – 601601Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_1000087631

Regions

Domain64 – 202139Flavodoxin-like
Domain236 – 450215FAD-binding FR-type
Nucleotide binding70 – 745FMN By similarity
Nucleotide binding117 – 1226FMN By similarity
Nucleotide binding150 – 18132FMN By similarity
Nucleotide binding388 – 3914FAD By similarity
Nucleotide binding422 – 4243FAD By similarity
Nucleotide binding521 – 5299NADP By similarity

Sites

Binding site4911NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ANX1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 93406AEFEFF5701A

FASTA60166,119
        10         20         30         40         50         60 
MTTQAPPSAL LPLNPEQLAR LQAATTDLSP TQLAWVSGYF WGMLNQQPGT LAATPAPVAE 

        70         80         90        100        110        120 
MPGITLISAS QTGNARRVAE ALRDDLLAAK LSVTLVNAGD YKFKQIANEK LLVVVASTQG 

       130        140        150        160        170        180 
EGEPPEEAVA LRKFLFSKKA PKLDNTAFAV FGLGDTSYEF FCQAGKDFDS KLAELGGERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAAQEWRAR VVDVLKARAP SASAAQVAVA ATGAVNDVHS SPYTKEAPLS 

       250        260        270        280        290        300 
ASLAVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPELVK EIVELVWLKG 

       310        320        330        340        350        360 
TEPVTVNGKV LPLAEALQWH FELTVNTANI VENYATLTRS ESLLPLVGDK AQLQHYAATT 

       370        380        390        400        410        420 
PIVDMLRFSP AQLDADALVG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RYEIEGRARA 

       430        440        450        460        470        480 
GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAADE 

       490        500        510        520        530        540 
APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKEKIYV QDKLREQGAE 

       550        560        570        580        590        600 
LWRWINDGAH IYVCGDANCM AKDVEQALLE VIAEFGGMDA EAADEFLSEL RVERRYQRDV 


Y

« Hide

References

[1]The Citrobacter koseri Genome Sequencing Project
McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000822 Genomic DNA. Translation: ABV15185.1.
RefSeqYP_001455620.1. NC_009792.1.

3D structure databases

ProteinModelPortalA8ANX1.
SMRA8ANX1. Positions 64-209, 228-601.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8ANX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5584181.
GenomeReviewsGene locus CKO_04119 in contig CP000822_GR.
KEGGcko:CKO_04119.
PATRIC20390575. VBICitKos71230_3449.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHBG736048.
OMAESADEYL.
ProtClustDBPRK10953.

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_CITK8
AccessionPrimary (citable) accession number: A8ANX1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 34 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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