Reviewed, UniProtKB/Swiss-Prot B4F234 (CYSI_PROMH)

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:	PMI2249

Organism

Proteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]

Taxonomic identifier

529507 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	576 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 576	576	Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540		PRO_1000146652
Sites
	Metal binding	435	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	441	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	480	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	484	1	Iron (siroheme axial ligand) By similarity
	Metal binding	484	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4F234-1 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 8ECE49A7C6B6FF05	FASTA	576	64,753
	10 20 30 40 50 60 MKSQTQAPLV VEGKLSDSER MKKESNFLRG TISDDLQNGL TGGFEGDNFL LIRFHGMYQQ 70 80 90 100 110 120 DDRDIRAERA QQLLEPRHAM MLRCRLPGGV ITPKQWLSID KFASENTLYG SIRITNRQTF 130 140 150 160 170 180 QFHGILKGHV KPAHQMLAST GLDALATAND VNRNVLCTSN PEQSSLHQEA YEWAKKLSEH 190 200 210 220 230 240 LLPRTHAYAE IWLDKEKVAT TDEEPILGET YLPRKFKTSV VIPPYNDVDL HANDMNFIAI 250 260 270 280 290 300 AENGHLVGFN VLVGGGLAMT HGDKKTFPRL ASEFGYIPID KTLAVAEAIV TTQRDWGNRT 310 320 330 340 350 360 ERKNAKTKYT LERVGIETFK QEVERRSGVM FDMIRPYQFT HRGDQIGWLK GVDNKWYLTL 370 380 390 400 410 420 FIESGRLIDK PNAPLKTGVA EIAKVHLGDF RLTANQNLIV AGVPEAQKEQ IEAIARQYGL 430 440 450 460 470 480 INDEVTPLRK HAMACVSFPT CPLAMAEAER FLPAFTDTLD NIMAKYGVSD EHIVVRVTGC 490 500 510 520 530 540 PNGCGRAMLA EVGLVGKAPD RYNLHLGGNR MGTRIPRMYR ENISSQEIIE ILDTLIGQWA 550 560 570 ISRELNEGFG DFLIRTDVIK PVVNSAIDFY EVQEVI

References

[1]

"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility." Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T. J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM942759 Genomic DNA. Translation: CAR44463.1.
RefSeq	YP_002151967.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6803372.
GenomeReviews	Gene locus PMI2249 in contig AM942759_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ITTTQWQ.
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_PROMH

Accession

Primary (citable) accession number: B4F234

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 23, 2008
Last modified:	November 3, 2009
This is version 12 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)