Reviewed, UniProtKB/Swiss-Prot A8A3P5 (CYSJ_ECOHS)

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:	EcHS_A2904

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [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	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
	Chain	1 – 599	599	Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541		PRO_1000087633
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)
	A8A3P5-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 16C59722178A85C0	FASTA	599	66,342
	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 QTAASEWRAR VVDALKSRAP VAAPSQSVAT GAVNEIHTSP YSKDSPLVAS 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 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

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV07149.1.
RefSeq	YP_001459532.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5592258.
GenomeReviews	Gene locus EcHS_A2904 in contig CP000802_GR.
KEGG	ecx:EcHS_A2904.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A8A3P5. FHKDGAL.
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_ECOHS

Accession

Primary (citable) accession number: A8A3P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 15 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)