Reviewed, UniProtKB/Swiss-Prot Q7VQH1 (CYSI_BLOFL)

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:	Bfl159

Organism

Blochmannia floridanus [Complete proteome] [HAMAP]

Taxonomic identifier

203907 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length	569 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
Technical term	Complete 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 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 – 569	569	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_0000199895
Sites
	Metal binding	433	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	439	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	478	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	482	1	Iron (siroheme axial ligand) By similarity
	Metal binding	482	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VQH1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 9F087CEF94BA2E6D	FASTA	569	64,902
	10 20 30 40 50 60 MIMLKYNNKL LSDNERIKKN SNFLRGTIEK DLDNNLTGGF NVDNAQLIRF HGMYQQDDRD 70 80 90 100 110 120 VRLERMNQKL EPLINMMLRC RLPGGVITSQ QWLNIDNFSE EQTLYSSIRL TTRQTFQLHG 130 140 150 160 170 180 ILKPKLKGIH QLLNKLGLDS IATAGDVNRN VICTANPMES KVHYQIWELS KKISEHLLPK 190 200 210 220 230 240 SKAYAEIWLN EKKIESIDSE PILSSVYLPR KFKIAIAVPP VNDVDVYAND LGLVAIKDNT 250 260 270 280 290 300 GNLIGFNVLI GGGLAMTYGD KSTYPRMASE FGYINLQDIL KIVESVITVQ RDWGDRYNRR 310 320 330 340 350 360 HAKTKYTLVK VGIDILKKEI ENRSGLKFSP MYPYKFTERG DKFGWIRGIN QDYWHLTLFI 370 380 390 400 410 420 ENGRVCNTSN ILIKKGLSEI AKVHSGFFRI TTNQNLIISE IHQDKKDIIE DLLKQYGLLG 430 440 450 460 470 480 DFVTSQRKSS MACVAFPTCP LAMAEAERFL PAFVTKVEHV MSKYNLQRDA IILRVTGCPN 490 500 510 520 530 540 GCARAMLAEI GLTGRGIGRY NLYLGGNKNG TRIPRLYKEN ITEDEILHVL DITIGDWAKN 550 560 RKTQESYGDY VVRAGIVRAV INSEEDFYL

References

[1]

"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes." Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248583 Genomic DNA. Translation: CAD83680.1.
RefSeq	NP_878465.1.
3D structure databases
SMR	Q7VQH1. Positions 77-568.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7VQH1.
Genome annotation databases
GeneID	1499359.
GenomeReviews	Gene locus Bfl159 in contig BX248583_GR.
KEGG	bfl:Bfl159.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0155.
HOGENOM	HBG626671.
OMA	PGDNSVD.
PhylomeDB	Q7VQH1.
Enzyme and pathway databases
BioCyc	CBLO203907:BFL159-MONOMER.
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. 2 hits. 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_BLOFL

Accession

Primary (citable) accession number: Q7VQH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 44 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)