Reviewed, UniProtKB/Swiss-Prot Q9KUX3 (CYSI_VIBCH)

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:	VC_0385

Organism

Vibrio cholerae [Complete proteome] [HAMAP]

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	577 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 – 577	577	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_0000199912
Sites
	Metal binding	440	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	446	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	486	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	490	1	Iron (siroheme axial ligand) By similarity
	Metal binding	490	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KUX3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: DB39CCC6AE14E2FD	FASTA	577	64,378
	10 20 30 40 50 60 MSANQNPSVQ EVLGEVLGPW SDNERLKRES HFLRGTIEQD LQDRITGGFT ADNFQLIRFH 70 80 90 100 110 120 GMYQQDDRDI RAERSKQKLE PLHNVMLRAR MPGGIITPHQ WLAIDKFATE HTLYGSIRLT 130 140 150 160 170 180 TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTSNPVESE LHLQAYEWAK 190 200 210 220 230 240 KISEHLLPKT RAYAEIWLDG EKIEGPDEEP ILGSNYLPRK FKTTVVIPPH NDVDVHANDL 250 260 270 280 290 300 NFVAIGENGQ LVGFNVLVGG GLAMTHGDTS TYPRRADDFG FIPLEKTLEV AAAVVSTQRD 310 320 330 340 350 360 WGNRSNRKNA KTKYTLDRVG VEVFKAEVEK RAGITFAPSR AYEFTSRGDR IGWVEGIDGK 370 380 390 400 410 420 HHLTLFIENG RILDFPGKPL KTGVAEIAKV HQGDFRMTAN QNLIVAGVPA DQKPHIEQLA 430 440 450 460 470 480 REHGLIDDGV SEQRINSMAC VAFPTCPLAM AEAERFLPSF VTEVEGILAK HALPKEENII 490 500 510 520 530 540 LRVTGCPNGC GRAMLAEIGL VGKAPGRYNL HLGGNRNGTR IPKMYKENIT DTQILQEIDE 550 560 570 LVGRWASERL DGEGFGDFTI RAGIIEEVII SKRDFYA

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF93558.1.
PIR	C82329.
RefSeq	NP_230039.1.
3D structure databases
SMR	Q9KUX3. Positions 86-576.
ModBase	Search...
Genome annotation databases
GeneID	2615028.
GenomeReviews	Gene locus VC_0385 in contig AE003852_GR.
KEGG	vch:VC0385.
TIGR	VC_0385.
Phylogenomic databases
HOGENOM	HBG626671.
OMA	PGDNSVD.
Enzyme and pathway databases
BRENDA	1.8.1.2. 19019.
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_VIBCH

Accession

Primary (citable) accession number: Q9KUX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 48 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)