Reviewed, UniProtKB/Swiss-Prot P38039 (CYSJ_SALTY)

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:	STM2948

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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. HAMAP MF_01541
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01541
Cofactor	Binds 1 FAD per subunit. HAMAP MF_01541 Binds 1 FMN per subunit. 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. HAMAP MF_01541
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_0000199935
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	117 – 122	6	FMN By similarity
	Nucleotide binding	150 – 181	32	FMN By similarity
	Nucleotide binding	386 – 389	4	FAD By similarity
	Nucleotide binding	420 – 422	3	FAD By similarity
	Nucleotide binding	519 – 527	9	NADP By similarity
Sites
	Binding site	489	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38039-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 13CBAC2BF806EBDB	FASTA	599	66,484
	10 20 30 40 50 60 MTTPAPLTGL LPLNPEQLAR LQAATTDLTP EQLAWVSGYF WGVLNPRSGA VAVTPVPERK 70 80 90 100 110 120 MPRVTLISAS QTGNARRVAE ALRDDLLAAN LNVTLVNAGD YKFKQIASEK LLVIVTSTQG 130 140 150 160 170 180 EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDTSYEF FCQSGKDFDS KLAELGGERL 190 200 210 220 230 240 LDRVDADVEY QAAASEWRAR VVDVLKSRAP VAAPSQSVAT GAVNDIHTSP YTKDAPLIAT 250 260 270 280 290 300 LSVNQKITGR NSEKDVRHIE IDLGDSGLRY QPGDALGVWY QNDPALVKEL VELLWLKGDE 310 320 330 340 350 360 PVTVDGKTLP LAEALEWHFE LTVNTANIVE NYATLTRSES LLPLVGDKAQ LQHYAATTPI 370 380 390 400 410 420 VDMVRFSPAQ LDAQALIDLL RPLTPRLYSI ASAQAEVESE VHITVGVVRY DIEGRARAGG 430 440 450 460 470 480 ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRSF MQQRAAEGVE 490 500 510 520 530 540 GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LSRIDLAWSR DQKEKIYVQD KLREQGAELW 550 560 570 580 590 RWINDGAHIY VCGDARRMAA DVEKALLEVI AEFGGMDLES ADEYLSELRV ERRYQRDVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase." Ostrowski J., Barber M.J., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15796-15808(1989) [PubMed: 2550423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase." Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15726-15737(1989) [PubMed: 2670946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 594-599. Strain: LT2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M23007 Genomic DNA. Translation: AAA27046.1. AE006468 Genomic DNA. Translation: AAL21828.1.
PIR	A34231.
RefSeq	NP_461869.1.
3D structure databases
HSSP	HSSP built from PDB template 1DDG based on UniProtKB P38038.
SMR	P38039. Positions 64-209, 226-599.
ModBase	Search...
Proteomic databases
PRIDE	P38039.
Genome annotation databases
GeneID	1254471.
GenomeReviews	Gene locus STM2948 in contig AE006468_GR.
KEGG	stm:STM2948.
NMPDR	fig|99287.1.peg.2844.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P38039.
OMA	EQLAWVS.
Enzyme and pathway databases
BioCyc	STYP99287:STM2948-MON.
BRENDA	1.8.1.2. 2.
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_SALTY

Accession

Primary (citable) accession number: P38039
Secondary accession number(s): P14782

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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