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P17846

- CYSI_ECOLI

UniProt

P17846 - CYSI_ECOLI

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Protein

Sulfite reductase [NADPH] hemoprotein beta-component

Gene

cysI

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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17846.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0155.
HOGENOMiHOG000218418.
InParanoidiP17846.
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

        10         20         30         40         50
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL
60 70 80 90 100
LIRFHGMYQQ DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID
110 120 130 140 150
KFAGENTIYG SIRLTNRQTF QFHGILKKNV KPVHQMLHSV GLDALATAND
160 170 180 190 200
MNRNVLCTSN PYESQLHAEA YEWAKKISEH LLPRTRAYAE IWLDQEKVAT
210 220 230 240 250
TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI AENGKLVGFN
260 270 280 290 300
LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT
310 320 330 340 350
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK
360 370 380 390 400
GIDDNWHLTL FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII
410 420 430 440 450
AGVPESEKAK IEKIAKESGL MNAVTPQREN SMACVSFPTC PLAMAEAERF
460 470 480 490 500
LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP NGCGRAMLAE VGLVGKAPGR
510 520 530 540 550
YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK EREAGEGFGD
560 570
FTVRAGIIRP VLDPARDLWD
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. Curated
The sequence CAA68816.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231H → L in AAA23651. (PubMed:2670946)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P17846.
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: November 26, 2014
This is version 143 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