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UniProtKB/Swiss-Prot entry A9LZ72


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYSI_NEIM0
Primary accession number A9LZ72
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on February 5, 2008 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 11)
Name and origin of the protein
Protein name Sulfite reductase [NADPH] hemoprotein beta-component
Synonyms SIR-HP
SIRHP
EC 1.8.1.2
Gene name
Name: cysI
OrderedLocusNames: NMCC_1069
From
Neisseria meningitidis serogroup C (strain 053442) [TaxID: 374833] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/j.ygeno.2007.10.004; PubMed=18031983 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q.;
"Characterization of ST-4821 complex, a unique Neisseria meningitidis clone.";
Genomics 91:78-87(2008).
Comments
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
CP000381; ABX73249.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001599205.1; -.
3D structure databases
ModBase A9LZ72.
Ontologies
GO
GO:0009337; Cellular component: sulfite reductase complex (NADPH) (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
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.
Graphical view of domain structure.
PRINTS PR00397; SIROHAEM.
TIGRFAMs TIGR02041; CysI; 1.
PROSITE PS00365; NIR_SIR; 1.
ProtoNet A9LZ72.
Genome annotation databases
GeneID 5796005; -.
GenomeReviews CP000381_GR; NMCC_1069.
KEGG nmn:NMCC_1069; -.
CMR A9LZ72; NMCC_1069.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   589  589     Sulfite reductase [NADPH] hemoprotein beta-component. PRO_1000087627
METAL   443   443        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   449   449        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   488   488        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   492   492        Iron (siroheme axial ligand) (By similarity). 
METAL   492   492        Iron-sulfur (4Fe-4S) (By similarity). 
Sequence information
Length: 589 AA [This is the length of the unprocessed precursor] Molecular weight: 66119 Da [This is the MW of the unprocessed precursor] CRC64: 3815FBB2C8CCAF34 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVQTKTKGL AWQEKPLSDN ERLKTESNFL RGTILDDLKD PLTGGFKGDN FQLIRFHGMY 

        70         80         90        100        110        120 
EQDDRDIRAE RAEAKLEPLK FMLLRCRLPG GIIKPSQWIE LDKFARENSH YRSIRLTNRQ 

       130        140        150        160        170        180 
TFQFHGVPKA KLQTMHRLLH KLGLDSIATA ADMNRNVLCT SNPIESELHR QAYEYAKKIS 

       190        200        210        220        230        240 
EHLLPRTRGY LDVWVDGKKV QSSDDFLQED EPILGKTYLP RKFKTAVVIP PLNDVDCYGN 

       250        260        270        280        290        300 
DLDFVAISDG NGQLAGFNVL AGGGLSMEHG NTKTYPNISL ELGFVPPEHA LKAAEAVVTT 

       310        320        330        340        350        360 
QRDFGNRSDR KNARTRYTIQ NMGLDNFRAE VERRMGMPFE PIRPFKFTGR GDRIGWVKGI 

       370        380        390        400        410        420 
DGNWHLTLFI ESGRLVDEGG KQLLTGVLEI AKIHKGDFRI TANQNLIVAN VAEADKAKIE 

       430        440        450        460        470        480 
ELARTYGLIR NDVSKLRENA MSCVSFPTCP LAMAEAERVL PDFIDELDKI MAKHGTSDDY 

       490        500        510        520        530        540 
IVTRITGCPN GCGRAMLAEI GLVGKAVERY NLHIGGDREG VRIPRLYKEN ITLPEILAEL 

       550        560        570        580 
DDLIGKWAAE RNIGEGFGDF AIRTGIVKPV LNAPVDFWDV SKAVAIARA 

A9LZ72 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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