Reviewed, UniProtKB/Swiss-Prot Q1R7T4 (CYSJ_ECOUT)

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:	UTI89_C3128

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
Cofactor	Binds 1 FAD per subunit By similarity. Binds 1 FMN per subunit By similarity.
Subunit structure	Alpha(8)-beta(8). 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: InterPro 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
	Chain	1 – 599	599	Sulfite reductase [NADPH] flavoprotein alpha-component		PRO_0000292966
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)
	Q1R7T4-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 9E957AD0872A050E	FASTA	599	66,312
	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 GTVNEIHTSP 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]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000243 Genomic DNA. Translation: ABE08580.1.
RefSeq	YP_542111.1.
3D structure databases
SMR	Q1R7T4. Positions 64-209, 226-599.
ModBase	Search...
Genome annotation databases
GeneID	3990453.
GenomeReviews	Gene locus UTI89_C3128 in contig CP000243_GR.
KEGG	eci:UTI89_C3128.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1R7T4.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C3128-MON.
Family and domain databases
HAMAP	MF_01541. [Tree]
InterPro	IPR010199. CysJ. IPR003097. FAD-binding_1. IPR001094. Flavdoxin_like. IPR008254. Flavodoxin/NO_synth. IPR001709. FPN_cyt_redctse. 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_ECOUT

Accession

Primary (citable) accession number: Q1R7T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	May 16, 2006
Last modified:	November 25, 2008
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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