Sulfite reductase [NADPH] flavoprotein alpha-component

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Q8X7U1 (CYSJ_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sulfite reductase [NADPH] flavoprotein alpha-component
Short name=SiR-FP
EC=1.8.1.2

Gene names

Name:	cysJ
Ordered Locus Names:	Z4074, ECs3619

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Electron transport Transport
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 599

598

Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541

PRO_0000199924

Regions

Domain

64 – 202

139

Flavodoxin-like

Domain

234 – 448

215

FAD-binding FR-type

Nucleotide binding

70 – 74

FMN By similarity

Nucleotide binding

117 – 122

FMN By similarity

Nucleotide binding

150 – 181

FMN By similarity

Nucleotide binding

386 – 389

FAD By similarity

Nucleotide binding

420 – 422

FAD By similarity

Nucleotide binding

519 – 527

NADP By similarity

Sites

Binding site

489

NADP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8X7U1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D6413B09B4BB0D22
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FASTA

599

66,382

        10         20         30         40         50         60 
MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE 

        70         80         90        100        110        120 
MPGITIISAS QTGNARRVAE ALRDDLLTAK LNVKLVNAGD YKFKQIASEK LLIVVTSTQG 

       130        140        150        160        170        180 
EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDSSYEF FCQSGKDFDS KLAELGGERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAASEWRAR VVDALKSRAP VAAPSQSVAT GVVNEIHTSP YSKDAPLVAS 

       250        260        270        280        290        300 
LSVNQKITGR NSEKDVRHIE IDLGDSGLRY QPGDALGVWY QNDPALVKEL VELLWLKGDE 

       310        320        330        340        350        360 
PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK LQHYAATTPI 

       370        380        390        400        410        420 
VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQEEVENE VHVTVGVVRY DVEGRARAGG 

       430        440        450        460        470        480 
ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRAF MQQRAADEAP 

       490        500        510        520        530        540 
GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LTRIDLAWSR DQKEKVYVQD KLREQGAELW 

       550        560        570        580        590 
RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY

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References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57872.1. BA000007 Genomic DNA. Translation: BAB37042.1.
PIR	C91081. D85926.
RefSeq	NP_289314.1. NC_002655.2. NP_311646.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X7U1.
SMR	Q8X7U1. Positions 59-599.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000024180; EBESCP00000023073; EBESCG00000023234. EBESCT00000060010; EBESCP00000057838; EBESCG00000059057.
GeneID	914659. 959221.
GenomeReviews	Gene locus Z4074 in contig AE005174_GR. Gene locus ECs3619 in contig BA000007_GR.
KEGG	ece:Z4074. ecs:ECs3619.
PATRIC	18356713. VBIEscCol44059_3539.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009975.
HOGENOM	HBG736048.
OMA	ESADEYL.
ProtClustDB	PRK10953.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3619-MONOMER.
Family and domain databases
HAMAP	MF_01541. CysJ. [Tree]
InterPro	IPR010199. 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]
Gene3D	G3DSA:1.20.990.10. NADPH_Cyt_P450_Rdtase_dom3. 1 hit.
KO	K00380.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMs	TIGR01931. CysJ. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSJ_ECO57

Accession

Primary (citable) accession number: Q8X7U1
Secondary accession number(s): Q7AB91

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents