Reviewed, UniProtKB/Swiss-Prot P52673 (CYSI_THIRO)

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

Thiocapsa roseopersicina

Taxonomic identifier

1058 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Thiocapsa

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540
Cofactor	Binds 1 siroheme per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
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.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_0000199911
Sites
	Metal binding	423	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	429	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	468	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	472	1	Iron (siroheme axial ligand) By similarity
	Metal binding	472	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52673-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6337D0DE9C941C70	FASTA	559	62,272
	10 20 30 40 50 60 MSAPIHENER IKARSNCLRG TLRESLADTL TGAISPEDTQ ISKFHGFYQQ DHRDRRQARP 70 80 90 100 110 120 EQYLEPYFGF MLRAPLPGGV CTPAQWLAID GMGRELGGGS LRLTTRQSFQ YHGILKRDIA 130 140 150 160 170 180 SVIRGINAVM IDSIGGCGDV NRNVLCNPNP VESALHREVY DWAKRISEHL LPRTRAYHEI 190 200 210 220 230 240 WLDGEQVGGG EDVEPIYGRT YLPRKFKTAV GVPPHNDVDV YANDLGFAAV ADGSRLIGFN 250 260 270 280 290 300 VSAGGTGRNT GIPATFPRLA DVLGFVEPER TLAVAEAVVT TQRHFGDRLD RTQARLKYTI 310 320 330 340 350 360 ERMGLDAFRD EVERRAGIRF APARPIGFTD QGDRTAWVRG QDGRWHLTLY IESGRLIDGP 370 380 390 400 410 420 GQSSMQGLRE IARIHQGDFR ITPNQNLIVA RVPEPGKSEI EALARKYGLL DKGIALRLNG 430 440 450 460 470 480 MSCVALPTCP LAMAEAERYY PDFLAQVERL TRKHGLAEQE IVTRMTGCPN GCARPYLAEL 490 500 510 520 530 540 ALVGKGPGRY NLMLGGNGRR YRLNRLYREN LDEAAILAEI DTLLGRYAAC RQPGERFGDY 550 LIRDGIVRPV VNPAEDFHE

References

[1]	"A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase." Bruehl A., Haverkamp T., Gisselmann G., Schwenn J.D. Biochim. Biophys. Acta 1295:119-124(1996) [PubMed: 8695637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 219 / 6311.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z23169 Genomic DNA. Translation: CAA80688.1.
PIR	S34191.
3D structure databases
HSSP	HSSP built from PDB template 7GEP based on UniProtKB P17846.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.2. 258176.
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...

Entry information

Entry name

CYSI_THIRO

Accession

Primary (citable) accession number: P52673

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 53 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)