NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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.
COFACTOR: Binds 1 FAD per subunit (By similarity).
COFACTOR: Binds 1 FMN per subunit (By similarity).
SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000003; BAB13126.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_240240.1; -.

3D structure databases

HSSP

P38038; 1DDG. [HSSP ENTRY / PDB]

ModBase

P57503.

Enzyme and pathway databases

BioCyc

BSP107806:BU428-MON; -.

Ontologies

GO:0004783;	Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01541; -; 1.
PBIL [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 of domain structure.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

TIGRFAMs

TIGR01931; cysJ; 1.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1109776; -.

GenomeReviews

BA000003_GR; BU428.

KEGG

buc:BU428; -.

Phylogenomic databases

HOGENOM

P57503; -.

Genome annotation databases

CMR

P57503; BU428.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 601`	`601`	`Sulfite reductase [NADPH] flavoprotein alpha-component.`	`PRO_0000199920`
`DOMAIN`	`65 203`	`139`	`Flavodoxin-like.`
`DOMAIN`	`236 450`	`215`	`FAD-binding FR-type.`
`NP_BIND`	`71 75`	`5`	`FMN (By similarity).`
`NP_BIND`	`151 182`	`32`	`FMN (By similarity).`
`NP_BIND`	`238 290`	`53`	`FAD (By similarity).`
`NP_BIND`	`474 601`	`128`	`NADP (By similarity).`

Sequence information

Length: 601 AA [This is the length of the unprocessed precursor]

Molecular weight: 69231 Da [This is the MW of the unprocessed precursor]

CRC64: A7BDD35F0CCF0E8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKNQNKFDPV FPLSSEQLNN LKELERTCTN IQSAWLSGYF WKIANQTSNI TSFQTNESEK 

        70         80         90        100        110        120 
NDPVITIISA SQTGNAKLLS KRLYEYFNKN NKISRLIDAM DYKFKKIKDE KILILIISTQ 

       130        140        150        160        170        180 
GEGEPPEEAL SFYKFIMSKN APNLNNLYYS VFGLGDTSYN LFCQAGKDFD KRFKELGGNS 

       190        200        210        220        230        240 
LLDRFDADIE YEDNYNKWSQ DLLQSINSKE KIYKSSVSYI DQENTLILSK NHYTKKNPAE 

       250        260        270        280        290        300 
GIILTNQKIT GRNSKKDVHH IEIDISNLNI KYSPGDALGV WYKNDSNLVK NILELLSINI 

       310        320        330        340        350        360 
SETITIKNDV ITIFDALQNH FELTNNTKNI IKSYANFSKN KFLKDIISND SDLENYTINT 

       370        380        390        400        410        420 
PLIKMIHDHP LKLSSQQLIG LLRPLTPRLY SISSSQEEID NEIHITVGVV KKLISGHVYL 

       430        440        450        460        470        480 
GGASGYLSQS LKSDDIIKIF IQTNDNFRLP INKNTPIIMI SSGTGIAPFR AFMQQRDNDN 

       490        500        510        520        530        540 
ADGKNWLFFG NPNFTEDFLY QVEWQKYIKK GLITNMNLAW SQDQKNKIYV QDRIRENSQE 

       550        560        570        580        590        600 
IWSWIEEGAQ IYVCGNASKM AKDVEKALLD IISHNAHLNL EESQEFLNNL RLNKRYKRDV 


Y

P57503 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools