Reviewed, UniProtKB/Swiss-Prot Q8VSR0 (CYSI_ACTPL)

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

Organism

Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)

Taxonomic identifier

715 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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 By similarity. HAMAP MF_01540
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540
Cofactor	Binds 1 siroheme per subunit By similarity. HAMAP MF_01540 Binds 1 4Fe-4S cluster per subunit By similarity. 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 By similarity. HAMAP MF_01540
Sequence similarities	Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
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 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 heme binding Inferred from electronic annotation. Source: InterPro 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
	Chain	1 – 588	588	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_0000199892
Sites
	Metal binding	442	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	448	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	487	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	491	1	Iron (siroheme axial ligand) By similarity
	Metal binding	491	1	Iron-sulfur (4Fe-4S) By similarity
Natural variations
	Natural variant	35	1	E → D in strain: AP213.
	Natural variant	40	1	G → D in strain: AP213.
	Natural variant	199	1	I → V in strain: AP213.
	Natural variant	218	1	F → Y in strain: AP213.
	Natural variant	250	1	D → E in strain: AP213.
	Natural variant	319	1	I → V in strain: AP213.
	Natural variant	373	1	G → V in strain: AP213.
	Natural variant	523	1	P → S in strain: AP213.

Sequences

	Sequence		Length	Mass (Da)
	Q8VSR0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 4CFE8C935664B2C2	FASTA	588	66,683
	10 20 30 40 50 60 MSDKKIKGLE WQEKPLSDNE RLKTDSNFLR GTILEDLKDG LTGGFKGDNF QLIRFHGMYE 70 80 90 100 110 120 QDDRDIRAER LEEKLEPLKF MLLRCRLPGG IIKPYQWIEI DKFAREHTRY QSIRLTNRQT 130 140 150 160 170 180 FQYHGVPKGK LQPMHRLLHS IGLDSIATAA DMNRNVLCTS NPIESELHQQ AYEFAKKISE 190 200 210 220 230 240 HLLPRSRGYL DVWVDGKKIE SSDDLLKIED EPILGKTFLP RKFKTAVAIP PLNDVDVYAN 250 260 270 280 290 300 DLNFIAIQDD NGQLCGFNVL VGGGLSFEHG NTKTYPNVAY SLGFVPLEHT LAAAEGVVKT 310 320 330 340 350 360 QRDFGNRSDR KNARVRYTIQ NMTLDGFRAE VERCMNIKFE PTRPYEFTER GDRIGWVKGI 370 380 390 400 410 420 DNNWHLTLFI ESGRITDKPE KPLMTGVLEL AKVHKGDFRI TANQNLIVAN VAEQDKAQIE 430 440 450 460 470 480 AIARQYGLIQ EISKLRENAM SCVSLPTCPL AMAEAERVLP DFISELDKVL SKHNVADESI 490 500 510 520 530 540 ITRITGCPNG CGRAMLAEIG LVGKAIGRYN LHIGGDRAGL RIPRLYKENI TLQEIVNEID 550 560 570 580 QLVARWATER QTNEAFGDFV IRSNIIAPVV NAHIDFWDAT KIIPTTII

References

[1]

"Cloning and characterization of the gene coding for NADPH-sulfite reductase hemoprotein from Actinobacillus pleuropneumoniae and use of the protein product as a vaccine." Willson P.J., Gerlach G.F., Klashinsky S., Potter A.A. Can. J. Vet. Res. 65:206-212(2001) [PubMed: 11768126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AP213 / Serotype 5a and AP37 / Serotype 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF378783 Genomic DNA. Translation: AAL48202.1. AF378784 Genomic DNA. Translation: AAL48203.1.
3D structure databases
SMR	Q8VSR0. Positions 82-578.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.2. 257522.
Family and domain databases
HAMAP	MF_01540. CysI. [Tree]
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.
TIGRFAMs	TIGR02041. CysI. 1 hit.
PROSITE	PS00365. NIR_SIR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSI_ACTPL

Accession

Primary (citable) accession number: Q8VSR0
Secondary accession number(s): Q8VSQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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