Reviewed, UniProtKB/Swiss-Prot Q8FEI7 (CYSJ_ECOL6)

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:	c3323

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [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	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 flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component By similarity.
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01541
Cofactor	Binds 1 FAD per subunit By similarity. Binds 1 FMN per subunit By similarity.
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: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 599	598	Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541		PRO_0000199925
Regions
	Domain	64 – 202	139	Flavodoxin-like
	Domain	234 – 448	215	FAD-binding FR-type
	Nucleotide binding	70 – 74	5	FMN By similarity
	Nucleotide binding	150 – 181	32	FMN By similarity
	Nucleotide binding	236 – 288	53	FAD By similarity
	Nucleotide binding	472 – 599	128	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FEI7-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DE270A69F72F0402	FASTA	599	66,282
	10 20 30 40 50 60 MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE 70 80 90 100 110 120 MPGITIISAS QTGNARRVAE ALRDDLLAAK 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 GAVNEIHTSP YSKDAPLAAS 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 ASSQAEVENE VHVTVGVVRY DVEGRARAGG 430 440 450 460 470 480 ASSFLADRVE EEGEVRVFIE HNDNFRLPTN PETPVIMIGP GTGIAPFRAF MQQRAADEAP 490 500 510 520 530 540 GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LTRIDLAWSR DQKEKIYVQD KLREQGAELW 550 560 570 580 590 RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN81772.1.
RefSeq	NP_755202.1.
3D structure databases
HSSP	HSSP built from PDB template 1DDG based on UniProtKB P38038.
SMR	Q8FEI7. Positions 63-208, 64-209, 225-598, 226-599.
ModBase	Search...
Genome annotation databases
GeneID	1039155.
GenomeReviews	Gene locus c3323 in contig AE014075_GR.
KEGG	ecc:c3323.
NMPDR	fig|199310.1.peg.3245.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8FEI7.
OMA	Q8FEI7. EQLAWVS.
Enzyme and pathway databases
BRENDA	1.8.1.2. 292881.
Family and domain databases
HAMAP	MF_01541. [Tree]
InterPro	IPR010199. CysJ. IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
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_ECOL6

Accession

Primary (citable) accession number: Q8FEI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 42 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)