P0C0B2 (CYSI_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative 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:	BUsg_412

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Protein existence	Uncertain

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-Rule MF_01540
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP-Rule 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-Rule 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.
Caution	Could be the product of a pseudogene.
Sequence caution	The sequence AE013218 differs from that shown. Reason: Frameshift at position 170.

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 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 binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro 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
	Chain	1 – 566	566	Putative sulfite reductase [NADPH] hemoprotein beta-component HAMAP-Rule MF_01540		PRO_0000199894
Sites
	Metal binding	430	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	436	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	475	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	479	1	Iron (siroheme axial ligand) By similarity
	Metal binding	479	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C0B2 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: E6F10AF8BC27F19C	FASTA	566	65,353
	10 20 30 40 50 60 MKKDYKKVFL KNTKEERIKE NSNYLRGTII DDLKDEITNG FTGDNFSLIR FHGMYQDDRD 70 80 90 100 110 120 LRLERNEQKL EPRYAMMLRC RLPRGIIKAK KWLKIDHFAS KNTLYGTIRL NNLQTFQFHG 130 140 150 160 170 180 ILKKTLKDAH KMLNKIGLDS LGTANDVNRN VLCTSNPMES LIHQQCYEWV SKISNFLLPQ 190 200 210 220 230 240 TKAYAEIWLN QKKIATTDQE PILGKTYLPR KFKTTVVVPP YNDVDLYAND MNFIAITKNN 250 260 270 280 290 300 KIVGFNVLIG GGLSINHGNK NTWPFLAVEL GYITLEKTLS VAESIVTTQR DWGNRTDRKN 310 320 330 340 350 360 AKTRYTIAKV GLSVFKKEVE KRANMTFETI KPYYFISRGD RFGWTKNINN DWSLTVFIQN 370 380 390 400 410 420 GRIYDNDKQL VKSGLLKIAN LHTGNFRLTA NQNIVISEIL DKNKKKIEEI AISHGLIKKV 430 440 450 460 470 480 SSLRENSMAC VSFPTCPLAI AESERILSFF ITKVENIMLK YGIEKEIIIL RISGCPNGCG 490 500 510 520 530 540 RSLLAEIGLI GKSLGRYNLY IGGNRIGSRI PKIYKENITE QEILIHLDFL IKIWSIERQK 550 560 KEHFGDFVIR RNVVKKVVNP IYDFWN

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. No translation available.
3D structure databases
ProteinModelPortal	P0C0B2.
SMR	P0C0B2. Positions 77-566.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	RNVMAPA.
Enzyme and pathway databases
UniPathway	UPA00140; UER00207.
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. 2 hits. 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...

Entry information

Entry name

CYSI_BUCAP

Accession

Primary (citable) accession number: P0C0B2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program