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P17846

- CYSI_ECOLI

UniProt

P17846 - CYSI_ECOLI

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Protein

Sulfite reductase [NADPH] hemoprotein beta-component

Gene
cysI, b2763, JW2733
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH.UniRule annotation

Cofactori

Binds 1 siroheme per subunit.
Binds 1 4Fe-4S cluster per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi434 – 4341Iron-sulfur (4Fe-4S)
Metal bindingi440 – 4401Iron-sulfur (4Fe-4S)
Metal bindingi479 – 4791Iron-sulfur (4Fe-4S)
Metal bindingi483 – 4831Iron (siroheme axial ligand)
Metal bindingi483 – 4831Iron-sulfur (4Fe-4S)

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  2. heme binding Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. NADP binding Source: InterPro
  5. sulfite reductase (NADPH) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cysteine biosynthetic process Source: UniProtKB-KW
  2. hydrogen sulfide biosynthetic process Source: UniProtKB-HAMAP
  3. sulfate assimilation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:BETACOMP-MONOMER.
ECOL316407:JW2733-MONOMER.
MetaCyc:BETACOMP-MONOMER.
UniPathwayiUPA00140; UER00207.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] hemoprotein beta-component (EC:1.8.1.2)
Short name:
SiR-HP
Short name:
SiRHP
Gene namesi
Name:cysI
Ordered Locus Names:b2763, JW2733
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10190. cysI.

Subcellular locationi

GO - Cellular componenti

  1. sulfite reductase complex (NADPH) Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 570569Sulfite reductase [NADPH] hemoprotein beta-componentUniRule annotationPRO_0000199896Add
BLAST

Proteomic databases

PaxDbiP17846.

Expressioni

Gene expression databases

GenevestigatoriP17846.

Interactioni

Subunit structurei

Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.

Protein-protein interaction databases

DIPiDIP-9380N.
IntActiP17846. 10 interactions.
STRINGi511145.b2763.

Structurei

Secondary structure

1
570
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 854
Helixi87 – 893
Beta strandi90 – 923
Helixi93 – 10614
Beta strandi107 – 1093
Beta strandi112 – 1143
Beta strandi120 – 1223
Turni127 – 1293
Helixi133 – 1386
Turni139 – 1413
Beta strandi143 – 1453
Turni147 – 1493
Helixi164 – 1663
Helixi167 – 18014
Turni205 – 2073
Beta strandi218 – 2214
Helixi230 – 2323
Beta strandi233 – 25321
Beta strandi272 – 2787
Helixi279 – 2813
Helixi282 – 29615
Helixi302 – 3043
Helixi307 – 3148
Helixi316 – 32712
Beta strandi347 – 3504
Beta strandi352 – 3543
Beta strandi355 – 3606
Helixi363 – 3653
Helixi375 – 38511
Beta strandi387 – 3926
Beta strandi398 – 4047
Helixi405 – 4073
Helixi408 – 41710
Turni418 – 4214
Helixi426 – 4294
Beta strandi431 – 4333
Turni437 – 4393
Turni448 – 4503
Helixi451 – 46414
Beta strandi474 – 4796
Helixi486 – 4883
Beta strandi489 – 4979
Beta strandi500 – 5056
Beta strandi509 – 5113
Beta strandi516 – 5238
Helixi524 – 54118
Helixi548 – 5547
Helixi564 – 5674

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOPX-ray1.60A74-570[»]
2AOPX-ray1.75A74-570[»]
2GEPX-ray1.90A74-570[»]
3AOPX-ray2.10A74-570[»]
3GEOX-ray2.10A74-570[»]
4AOPX-ray1.80A74-570[»]
4G38X-ray1.56A1-570[»]
4G39X-ray2.40A1-570[»]
4GEPX-ray2.00A74-570[»]
4HTRX-ray1.60A64-570[»]
5AOPX-ray2.20A74-570[»]
5GEPX-ray2.10A74-570[»]
6GEPX-ray1.80A74-570[»]
7GEPX-ray2.40A74-570[»]
8GEPX-ray2.20A74-570[»]
ProteinModelPortaliP17846.
SMRiP17846. Positions 81-570.

Miscellaneous databases

EvolutionaryTraceiP17846.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0155.
HOGENOMiHOG000218418.
KOiK00381.
OMAiELHQEAY.
OrthoDBiEOG6W9XFB.
PhylomeDBiP17846.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
HAMAPiMF_01540. CysI.
InterProiIPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamiPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
TIGRFAMsiTIGR02041. CysI. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17846-1 [UniParc]FASTAAdd to Basket

« Hide

MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL    50
LIRFHGMYQQ DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID 100
KFAGENTIYG SIRLTNRQTF QFHGILKKNV KPVHQMLHSV GLDALATAND 150
MNRNVLCTSN PYESQLHAEA YEWAKKISEH LLPRTRAYAE IWLDQEKVAT 200
TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI AENGKLVGFN 250
LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT 300
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK 350
GIDDNWHLTL FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII 400
AGVPESEKAK IEKIAKESGL MNAVTPQREN SMACVSFPTC PLAMAEAERF 450
LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP NGCGRAMLAE VGLVGKAPGR 500
YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK EREAGEGFGD 550
FTVRAGIIRP VLDPARDLWD 570
Length:570
Mass (Da):63,998
Last modified:January 23, 2007 - v4
Checksum:i03B41FEE6AB349C6
GO

Sequence cautioni

The sequence AAA23651.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA68816.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231H → L in AAA23651. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23008 Genomic DNA. Translation: AAA23651.1. Different initiation.
U29579 Genomic DNA. Translation: AAA69273.1.
U00096 Genomic DNA. Translation: AAC75805.1.
AP009048 Genomic DNA. Translation: BAE76840.1.
Y07525 Genomic DNA. Translation: CAA68816.1. Different initiation.
PIRiG65057. RDECSH.
RefSeqiNP_417243.1. NC_000913.3.
YP_490972.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75805; AAC75805; b2763.
BAE76840; BAE76840; BAE76840.
GeneIDi12933282.
947231.
KEGGiecj:Y75_p2701.
eco:b2763.
PATRICi32120938. VBIEscCol129921_2861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23008 Genomic DNA. Translation: AAA23651.1 . Different initiation.
U29579 Genomic DNA. Translation: AAA69273.1 .
U00096 Genomic DNA. Translation: AAC75805.1 .
AP009048 Genomic DNA. Translation: BAE76840.1 .
Y07525 Genomic DNA. Translation: CAA68816.1 . Different initiation.
PIRi G65057. RDECSH.
RefSeqi NP_417243.1. NC_000913.3.
YP_490972.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOP X-ray 1.60 A 74-570 [» ]
2AOP X-ray 1.75 A 74-570 [» ]
2GEP X-ray 1.90 A 74-570 [» ]
3AOP X-ray 2.10 A 74-570 [» ]
3GEO X-ray 2.10 A 74-570 [» ]
4AOP X-ray 1.80 A 74-570 [» ]
4G38 X-ray 1.56 A 1-570 [» ]
4G39 X-ray 2.40 A 1-570 [» ]
4GEP X-ray 2.00 A 74-570 [» ]
4HTR X-ray 1.60 A 64-570 [» ]
5AOP X-ray 2.20 A 74-570 [» ]
5GEP X-ray 2.10 A 74-570 [» ]
6GEP X-ray 1.80 A 74-570 [» ]
7GEP X-ray 2.40 A 74-570 [» ]
8GEP X-ray 2.20 A 74-570 [» ]
ProteinModelPortali P17846.
SMRi P17846. Positions 81-570.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9380N.
IntActi P17846. 10 interactions.
STRINGi 511145.b2763.

Proteomic databases

PaxDbi P17846.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75805 ; AAC75805 ; b2763 .
BAE76840 ; BAE76840 ; BAE76840 .
GeneIDi 12933282.
947231.
KEGGi ecj:Y75_p2701.
eco:b2763.
PATRICi 32120938. VBIEscCol129921_2861.

Organism-specific databases

EchoBASEi EB0187.
EcoGenei EG10190. cysI.

Phylogenomic databases

eggNOGi COG0155.
HOGENOMi HOG000218418.
KOi K00381.
OMAi ELHQEAY.
OrthoDBi EOG6W9XFB.
PhylomeDBi P17846.

Enzyme and pathway databases

UniPathwayi UPA00140 ; UER00207 .
BioCyci EcoCyc:BETACOMP-MONOMER.
ECOL316407:JW2733-MONOMER.
MetaCyc:BETACOMP-MONOMER.

Miscellaneous databases

EvolutionaryTracei P17846.
PROi P17846.

Gene expression databases

Genevestigatori P17846.

Family and domain databases

Gene3Di 3.90.480.10. 2 hits.
HAMAPi MF_01540. CysI.
InterProi IPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view ]
Pfami PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view ]
PRINTSi PR00397. SIROHAEM.
SUPFAMi SSF55124. SSF55124. 2 hits.
TIGRFAMsi TIGR02041. CysI. 1 hit.
PROSITEi PS00365. NIR_SIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: B.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli."
    Krone F.A., Westphal G., Schwenn J.D.
    Mol. Gen. Genet. 225:314-319(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-570.
    Strain: K12.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  6. "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions."
    Crane B.R., Siegel L.M., Getzoff E.D.
    Science 270:59-67(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  7. "Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange."
    Crane B.R., Siegel L.M., Getzoff E.D.
    Biochemistry 36:12101-12119(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiCYSI_ECOLI
AccessioniPrimary (citable) accession number: P17846
Secondary accession number(s): Q2MA66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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