Reviewed, UniProtKB/Swiss-Prot Q8K9D3 (CYSJ_BUCAP)

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:	BUsg_413

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	602 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 – 602	602	Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541		PRO_0000199921
Regions
	Domain	68 – 206	139	Flavodoxin-like
	Domain	237 – 451	215	FAD-binding FR-type
	Nucleotide binding	74 – 78	5	FMN By similarity
	Nucleotide binding	154 – 185	32	FMN By similarity
	Nucleotide binding	239 – 291	53	FAD By similarity
	Nucleotide binding	475 – 602	128	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9D3-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: FA3793147889B7B3	FASTA	602	69,930
	10 20 30 40 50 60 MKNKNPFNIF FPLSLDKIEN LEKIKKNCSS IQYAWLSGYF WNLANQTPSR LICEKNEFFR 70 80 90 100 110 120 KDNEEKIITI ISASQTGNAR QLAKRFNKYL KNENKKTNLI DAADYNFKKI KNERFLILII 130 140 150 160 170 180 STQGEGEPPE EALSFYKFIM SKKAPRLENL HYSVFGLGDV SYNLFCQAGK DFDKRFSELG 190 200 210 220 230 240 GKSLLHRLDS DIEYESNYIQ WSEELLLAIN KIDVSTCSVF KKNDKKNFID KLNYTKYKPA 250 260 270 280 290 300 VATVLLNQKI TGRNSTKDVH HIELDITNSN IVYTPGDALG VWYQNSSQLI KQILKLLSIR 310 320 330 340 350 360 ISDKVKVKDK IITIFEALKK NFELTTNTKH IIQKYTDVTQ NKFLKKIISD NKKLNNYVKK 370 380 390 400 410 420 TPLLKMIYDH PKKLSSQQLI SILRPLKPRL YSISSSQSEM NDEVHITVGV VKKQISGTIH 430 440 450 460 470 480 LGGSSSYLSQ FLKIDDSVKI FVEEKSNFRL PENKDVPIIM IGSGTGIAPF RAFIQQRDND 490 500 510 520 530 540 KATGKNWIFF GNPNFTEDFL YQLEWQKYLK KKLLTKMSLA WSRDQKEKIY VQDKIRENGK 550 560 570 580 590 600 ELWEWVNQGA QIYVCGNASK MAKDVEKELL DVFSKNGSMD IEESSEFLNN LRITRRYQRD VY

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67958.1.
RefSeq	NP_660747.1.
3D structure databases
HSSP	HSSP built from PDB template 1DDG based on UniProtKB P38038.
ModBase	Search...
Genome annotation databases
GeneID	1005748.
GenomeReviews	Gene locus BUsg_413 in contig AE013218_GR.
KEGG	bas:BUsg413.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8K9D3.
OMA	Q8K9D3. EQLAWVS.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG413-MON.
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_BUCAP

Accession

Primary (citable) accession number: Q8K9D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 51 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)