Sulfite reductase [NADPH] hemoprotein beta-component

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Reviewed, UniProtKB/Swiss-Prot P17846 (CYSI_ECOLI)

Last modified November 3, 2009. Version 102. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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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.

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

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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
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation Inferred from electronic annotation. Source: HAMAP
Cellular component	sulfite reductase complex (NADPH) Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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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 MF_01540

PRO_0000199896

Sites

Metal binding

434

Iron-sulfur (4Fe-4S) HAMAP MF_01540

Metal binding

440

Iron-sulfur (4Fe-4S) HAMAP MF_01540

Metal binding

479

Iron-sulfur (4Fe-4S) HAMAP MF_01540

Metal binding

483

Iron (siroheme axial ligand) HAMAP MF_01540

Metal binding

483

Iron-sulfur (4Fe-4S) HAMAP MF_01540

Experimental info

Sequence conflict

H → L in AAA23651. Ref.1

Secondary structure

570

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P17846-1 [UniParc].

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

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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: 2670946] [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: 9278503] [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: 16738553] [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: 2005873] [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: 9298646] [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: 7569952] [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: 9315848] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

AP_003330.1.
NP_417243.1.

3D structure databases

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	[»]
4GEP	X-ray	2.00	A	74-570	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9380N.

STRING

P17846.

Genome annotation databases

GeneID

947231.

GenomeReviews

Gene locus JW2733 in contig AP009048_GR.
Gene locus b2763 in contig U00096_GR.

KEGG

ecj:JW2733.
eco:b2763.

Organism-specific databases

EchoBASE

EB0187.

EcoGene

EG10190. cysI.

CMR

Search...

Phylogenomic databases

HOGENOM

P17846.

OMA

ITTTQWQ.

Enzyme and pathway databases

BioCyc

EcoCyc:BETACOMP-MON.
MetaCyc:BETACOMP-MON.

Gene expression databases

Genevestigator

P17846.

Family and domain databases

HAMAP

MF_01540.
[Tree]

InterPro

IPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S.
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.

TIGRFAMs

TIGR02041. CysI. 1 hit.

PROSITE

PS00365. NIR_SIR. 1 hit.
[Graphical view]

ProtoNet

Search...

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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:	November 3, 2009
This is version 102 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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