NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
DOI=10.1038/nbt1045; PubMed=15592456 [NCBI, ExPASy, EBI, Israel, Japan]
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4.";
Nat. Biotechnol. 23:63-68(2005).

Comments

FUNCTION: This enzyme 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.
COFACTOR: Binds 1 siroheme per subunit (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
SUBUNIT: Alpha(8)-beta(4). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE008692; AAV88632.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_161743.1; -.

3D structure databases

SMR

Q5NRM2; 81-570.

ModBase

Q5NRM2.

Enzyme and pathway databases

BioCyc

ZMOB264203:ZMO0008-MON; -.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004783;	Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0019344;	Biological process: cysteine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01540; -; 1.
PBIL [Tree]

InterPro

IPR011786; CysI.
IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
Graphical view of domain structure.

Pfam

PF01077; NIR_SIR; 1.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.

PR00397; SIROHAEM.

TIGR02041; CysI; 1.

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

3189461; -.

GenomeReviews

AE008692_GR; ZMO0008.

KEGG

zmo:ZMO0008; -.

NMPDR

fig|264203.3.peg.504; -.

Phylogenomic databases

HOGENOM

Q5NRM2; -.

Genome annotation databases

CMR

Q5NRM2; ZMO0008.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 570`	`570`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_0000199919`
`METAL`	`434 434`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`440 440`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`479 479`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`483 483`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`483 483`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 570 AA [This is the length of the unprocessed precursor]

Molecular weight: 64064 Da [This is the MW of the unprocessed precursor]

CRC64: BA050FC80FC53326 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQKHPQTLV VDAPLSDAER LKRESNFLRG TIAEDLNDGL TGGFNGDNST LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA EEKLEPRYAM MLRCRLPGGI ISPEQWLKMD SFASEKTLYG SIRLTNRQTF 

       130        140        150        160        170        180 
QFHGILKKDL KTVHHLLHES GLDSLATAND VNRNVLCTSN PVESDLHAEA YEWAKKISEH 

       190        200        210        220        230        240 
LLPQTHAYAE IWLDQEKLAT TDQEPILGAT YLPRKFKTTV VIPPQNDVDI YANDLNFIAI 

       250        260        270        280        290        300 
SENDQLVGFN VLIGGGLSIT IGDKTTHPGV AKDIGYIEKE KVLAVAEAVV TTQRDWGNRS 

       310        320        330        340        350        360 
NRKNARLRYT LERVGLDVFK AEVEKRAGVT FEASRPFTLT GRGDRFGWVK GIDNQWHLTL 

       370        380        390        400        410        420 
FVENGRLLDY PHRPLKSGIA EIAKVHKGDF RLTANQNLIV AGVSEEDKDT IEKIARDHGL 

       430        440        450        460        470        480 
LENISELRKN SMACVSFPTC PLAMAEAERF LPNFLTKVEA VMTKYDIADE YIVFRTTGCP 

       490        500        510        520        530        540 
NNCGRSLLAE IGLVGRAIGR YNLYIGGDRV GTRIPRLFRE NITEDEILSE VDSLIGRWAK 

       550        560        570 
ERDGKEAFGD FVVRAGIVKA VTDPAIDFYD

Q5NRM2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools