Reviewed, UniProtKB/Swiss-Prot A1RGD7 (CYSI_SHESW)

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:	Sputw3181_0882

Organism

Shewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]

Taxonomic identifier

351745 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	565 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 – 565	565	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_1000068774
Sites
	Metal binding	429	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	435	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	474	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	478	1	Iron (siroheme axial ligand) By similarity
	Metal binding	478	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1RGD7-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: E36896A650CA30D1	FASTA	565	62,996
	10 20 30 40 50 60 MSEQKLALNE YLKTDSDYLR GTIKEGLDSS VTGSFSDGDQ QLIKFHGFYQ QDDRDLRNER 70 80 90 100 110 120 KEQKLEPLYS FMLRARVPGG ICTPQQWLGV DKIASTLTSS NSIRLTTRQT FQYHGIPKRN 130 140 150 160 170 180 LKTIIQDLDR QALDSIAACG DVNRNVMCNP NPVESKLHEQ AYAVAKKLSD HLLPHTRAYA 190 200 210 220 230 240 EIWLDEEKLL TTEDETVEPV YGKTYLPRKF KMAVAVPPDN DVDVYTNDLG FIAVAENGEL 250 260 270 280 290 300 VGFNLTAGGG MGSTHGEVET FPRLADDFGF IKTEDVMKFA EAVMTVQRDW GNRSNRKRSR 310 320 330 340 350 360 LKYTIVDHGY EKFKAEVEAR AGVKFEPKRD VVIGDRGDRY GWVEGVDGKW HLTLFIESGR 370 380 390 400 410 420 IKDLPGQTLQ TGLREIAKIH KGDFRMTSNQ NMIIAGVAAE DKATIEGLAR KHGLLGQVLT 430 440 450 460 470 480 QTRGHSIACV ALPTCPLAMA EAERYFPEFI DHIDALQAKH GISEQAIVVR MTGCPNGCAR 490 500 510 520 530 540 PFAAEIGLVG KAPGRYNLYL GASFEGTRLN KMHRENIQEA DILAELDTLF GRYAVERDAG 550 560 ETFGNFTVRV GVVKAVIDAA KDFHG

References

[1]

"Complete sequence of Shewanella sp. W3-18-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000503 Genomic DNA. Translation: ABM23732.1.
RefSeq	YP_962286.1.
3D structure databases
SMR	A1RGD7. Positions 72-564.
ModBase	Search...
Protein-protein interaction databases
STRING	A1RGD7.
Genome annotation databases
GeneID	4657907.
GenomeReviews	Gene locus Sputw3181_0882 in contig CP000503_GR.
KEGG	shw:Sputw3181_0882.
NMPDR	fig|351745.7.peg.830.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0155.
HOGENOM	HBG626671.
OMA	PGDNSVD.
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_SHESW

Accession

Primary (citable) accession number: A1RGD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
Last modified:	February 9, 2010
This is version 25 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)