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ECOLI:CYSJ

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cysJ (ECO:0000255 with HAMAP-Rule:MF_01541)
Protein Name(s) Sulfite reductase [NADPH] flavoprotein alpha-component (ECO:0000255 with HAMAP-Rule:MF_01541)

SiR-FP (ECO:0000255 with HAMAP-Rule:MF_01541)

External Links
UniProt P38038
EMBL M23008
U29579
U00096
AP009048
PIR H65057
RefSeq NP_417244.1
WP_000211913.1
PDB 1DDG
1DDI
1YKG
PDBsum 1DDG
1DDI
1YKG
DisProt DP00190
ProteinModelPortal P38038
SMR P38038
BioGrid 4262283
DIP DIP-9381N
IntAct P38038
MINT MINT-1239442
STRING 511145.b2764
DrugBank DB03147
EPD P38038
PaxDb P38038
EnsemblBacteria AAC75806
BAE76841
GeneID 947239
KEGG ecj:JW2734
eco:b2764
PATRIC 32120940
EchoBASE EB0188
EcoGene EG10191
eggNOG ENOG4107EER
COG0369
HOGENOM HOG000282025
InParanoid P38038
KO K00380
OMA GVWYEND
OrthoDB EOG6CVV7G
PhylomeDB P38038
BioCyc EcoCyc:ALPHACOMP-MONOMER
ECOL316407:JW2734-MONOMER
MetaCyc:ALPHACOMP-MONOMER
BRENDA 1.8.1.2
UniPathway UPA00140
EvolutionaryTrace P38038
PRO PR:P38038
Proteomes UP000000318
UP000000625
GO GO:0009337
GO:0050660
GO:0010181
GO:0005506
GO:0042602
GO:0004783
GO:0019344
GO:0070814
GO:0000103
Gene3D 1.20.990.10
3.40.50.360
HAMAP MF_01541
InterPro IPR010199
IPR029758
IPR003097
IPR017927
IPR001094
IPR008254
IPR001709
IPR029039
IPR023173
IPR001433
IPR017938
Pfam PF00667
PF00258
PF00175
PIRSF PIRSF000207
PRINTS PR00369
PR00371
SUPFAM SSF52218
SSF63380
TIGRFAMs TIGR01931
PROSITE PS51384
PS50902

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009055

electron carrier activity

other:GO_REF:0000100

ECO:0000247

PMID:2334437[1]


F

The transfer annotation HHpred hits had an E-value of 1.7E-28, a similarity of 100%, and a query coverage of 94.12% which serves as the evidence.

complete
CACAO 12045

enables

GO:0070401

NADP+ binding

PMID:10860732[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:10860732[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10191
MGI:MGI:97361
PANTHER:PTN000453956
RGD:3184
RGD:68335
UniProtKB:O08336
UniProtKB:O08394
UniProtKB:Q9UBK8
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97744
PANTHER:PTN000453956
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10191
MGI:MGI:97361
PANTHER:PTN000453956
RGD:3184
RGD:68335
UniProtKB:O08336
UniProtKB:O08394
UniProtKB:Q9UBK8
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453956
RGD:3184
RGD:3185
RGD:3186
UniProtKB:P35228
UniProtKB:Q9SB48
UniProtKB:Q9UHB4

C

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:7657631[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042602

riboflavin reductase (NADPH) activity

PMID:7657631[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

PMID:7657631[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009337

sulfite reductase complex (NADPH)

PMID:8360156[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000103

sulfate assimilation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029758

P

Seeded From UniProt

complete

enables

GO:0004783

sulfite reductase (NADPH) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010199
InterPro:IPR029758

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001094
InterPro:IPR008254
InterPro:IPR010199
InterPro:IPR029758

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR003097
InterPro:IPR017927
InterPro:IPR023173

F

Seeded From UniProt

complete

involved_in

GO:0019344

cysteine biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010199
InterPro:IPR029758

P

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010199
InterPro:IPR029758

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001094
InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR003097
InterPro:IPR010199
InterPro:IPR017927
InterPro:IPR023173
InterPro:IPR029758

P

Seeded From UniProt

complete

enables

GO:0004783

sulfite reductase (NADPH) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.1.2

F

Seeded From UniProt

complete

enables

GO:0004783

sulfite reductase (NADPH) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079062

F

Seeded From UniProt

complete

involved_in

GO:0070814

hydrogen sulfide biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079062

P

Seeded From UniProt

complete

involved_in

GO:0000103

sulfate assimilation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079062

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0249
UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0019344

cysteine biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0198

P

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

involved_in

GO:0070814

hydrogen sulfide biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00140

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Helms, LR et al. (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168 809-17 PubMed GONUTS page
  2. 2.0 2.1 Gruez, A et al. (2000) Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. J. Mol. Biol. 299 199-212 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. 4.0 4.1 4.2 Eschenbrenner, M et al. (1995) The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. J. Biol. Chem. 270 20550-5 PubMed GONUTS page
  5. Covès, J et al. (1993) NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 268 18604-9 PubMed GONUTS page