ID   CYSI_NEIMF              Reviewed;         589 AA.
AC   A1KU05;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE            Short=SIR-HP;
DE            Short=SIRHP;
DE            EC=1.8.1.2;
GN   Name=cysI; OrderedLocusNames=NMC1091;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 /
OS   FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C.,
RA   Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E.,
RA   Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S.,
RA   Unwin L., Whitehead S., Quail M.A., Achtman M., Barrell B.G.,
RA   Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
CC   -!- FUNCTION: This enzyme catalyzes the 6-electron reduction of
CC       sulfite to sulfide. This is one of several activities required for
CC       the biosynthesis of L-cysteine from sulfate (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH.
CC   -!- COFACTOR: Binds 1 siroheme per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SUBUNIT: Alpha(8)-beta(4). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; AM421808; CAM10346.1; -; Genomic_DNA.
DR   RefSeq; YP_975134.1; -.
DR   GeneID; 4676437; -.
DR   GenomeReviews; AM421808_GR; NMC1091.
DR   KEGG; nmc:NMC1091; -.
DR   NMPDR; fig|487.2.peg.2214; -.
DR   OMA; A1KU05; ITTTQWQ.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:HAMAP.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_01540; -; 1.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   TIGRFAMs; TIGR02041; CysI; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    589       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000068766.
FT   METAL       443    443       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       449    449       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       488    488       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       492    492       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       492    492       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   589 AA;  65964 MW;  8659C0997E0CE46B CRC64;
     MTVQTKTKGL AWQEKPLSDN ERLKTESNFL RGTILDDLKD PLTGGFKGDN FQLIRFHGMY
     EQDDRDIRAE RAEAKLEPLK FMLLRCRLPG GIIKPSQWIE LDKFARENSH YRSIRLTNRQ
     TFQFHGVPKA KLQTMHRLLH KLGLDSIATA ADMNRNVLCT SNPIESELHR QAYEYAKKIS
     EHLLPRTRGY LDVWVDGKKV QSSDDFLQED EPILGKTYLP RKFKTAVVIP PLNDVDCYGN
     DLDFVAVSDG NGQLAGFNVL AGGGLSMEHG NTKTYPNISL ELGFVPPEHA LKAAEAVVTT
     QRDFGNRSDR KNARTRYTIQ NMGLDNFRAE VERRMGMPFE PIRPFKFTGR GDRIGWVKGI
     DGNWHLTLFI ESGRLVDEGG KQLLTGVLEI AKIHKGDFRI TANQNLIVAN VAEADKAKIE
     ELARTYGLIR NDVSKLRENA MSCVSFPTCP LAMAEAERVL PDFIGELDKI MAKHGTSDDY
     IVTRITGCPN GCGRAMLAEI GLVGKAVGRY NLHIGGDREG VRIPRLYKEN ITLPEILSEL
     DDLIGKWAAG RDTDEGFGDF AIRTGIVKPV LDAPVDFWDA SKAVPIARA
//