Sulfite reductase [NADPH] hemoprotein beta-component

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P17846 (CYSI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sulfite reductase [NADPH] hemoprotein beta-component
Short name=SiR-HP
Short name=SiRHP
EC=1.8.1.2

Gene names

Name:	cysI
Ordered Locus Names:	b2763, JW2733

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP-Rule MF_01540
Catalytic activity	H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH. HAMAP-Rule MF_01540
Cofactor	Binds 1 siroheme per subunit. Binds 1 4Fe-4S cluster per subunit.
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP-Rule MF_01540
Subunit structure	Alpha(8)-beta₈. The alpha component is a flavoprotein, the beta component is a hemoprotein.
Sequence similarities	Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Sequence caution	The sequence AAA23651.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA68816.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW hydrogen sulfide biosynthetic process Inferred from electronic annotation. Source: HAMAP sulfate assimilation Inferred from electronic annotation. Source: HAMAP
Cellular_component	sulfite reductase complex (NADPH) Inferred from direct assay PubMed 8360156. Source: EcoCyc
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay PubMed 6257697. Source: EcoCyc NADP binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from direct assay PubMed 6257697. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Initiator methionine

Removed Ref.5

Chain

2 – 570

569

Sulfite reductase [NADPH] hemoprotein beta-component HAMAP-Rule MF_01540

PRO_0000199896

Sites

Metal binding

434

Iron-sulfur (4Fe-4S)

Metal binding

440

Iron-sulfur (4Fe-4S)

Metal binding

479

Iron-sulfur (4Fe-4S)

Metal binding

483

Iron (siroheme axial ligand)

Metal binding

483

Iron-sulfur (4Fe-4S)

Experimental info

Sequence conflict

H → L in AAA23651. Ref.1

Secondary structure

570

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P17846 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 03B41FEE6AB349C6
Show »

FASTA

570

63,998

        10         20         30         40         50         60 
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAGENTIYG SIRLTNRQTF 

       130        140        150        160        170        180 
QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH 

       190        200        210        220        230        240 
LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI 

       250        260        270        280        290        300 
AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT 

       310        320        330        340        350        360 
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDNWHLTL 

       370        380        390        400        410        420 
FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII AGVPESEKAK IEKIAKESGL 

       430        440        450        460        470        480 
MNAVTPQREN SMACVSFPTC PLAMAEAERF LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP 

       490        500        510        520        530        540 
NGCGRAMLAE VGLVGKAPGR YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK 

       550        560        570 
EREAGEGFGD FTVRAGIIRP VLDPARDLWD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

RDECSH. G65057.

RefSeq

NP_417243.1. NC_000913.2.
YP_490972.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P17846.

SMR

P17846. Positions 81-570.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9380N.

IntAct

P17846. 10 interactions.

STRING

511145.b2763.

Proteomic databases

PaxDb

P17846.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75805; AAC75805; b2763.
BAE76840; BAE76840; BAE76840.

GeneID

12933282.
947231.

KEGG

ecj:Y75_p2701.
eco:b2763.

PATRIC

32120938. VBIEscCol129921_2861.

Organism-specific databases

EchoBASE

EB0187.

EcoGene

EG10190. cysI.

Phylogenomic databases

eggNOG

COG0155.

HOGENOM

HOG000218418.

K00381.

OMA

RNVMAPA.

ProtClustDB

PRK13504.

Enzyme and pathway databases

BioCyc

EcoCyc:BETACOMP-MONOMER.
ECOL316407:JW2733-MONOMER.
MetaCyc:BETACOMP-MONOMER.

UniPathway

UPA00140; UER00207.

Gene expression databases

Genevestigator

P17846.

Family and domain databases

Gene3D

3.90.480.10. 2 hits.

HAMAP

MF_01540. CysI.

InterPro

IPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]

Pfam

PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]

PRINTS

PR00397. SIROHAEM.

SUPFAM

SSF55124. NiR_SiRalpha_1/3. 2 hits.

TIGRFAMs

TIGR02041. CysI. 1 hit.

PROSITE

PS00365. NIR_SIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17846.

Entry information

Entry name

CYSI_ECOLI

Accession

Primary (citable) accession number: P17846
Secondary accession number(s): Q2MA66

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 133 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents