ID   CYSI_XANAC              Reviewed;         568 AA.
AC   Q8PHC8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-OCT-2013, entry version 71.
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=XAC3331;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Component of the sulfite reductase complex that
CC       catalyzes the 6-electron reduction of sulfite to sulfide. This is
CC       one of several activities required for the biosynthesis of L-
CC       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   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC       hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC   -!- SUBUNIT: Alpha(8)-beta(8). 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; AE008923; AAM38174.1; -; Genomic_DNA.
DR   RefSeq; NP_643638.1; NC_003919.1.
DR   ProteinModelPortal; Q8PHC8; -.
DR   STRING; 190486.XAC3331; -.
DR   EnsemblBacteria; AAM38174; AAM38174; XAC3331.
DR   GeneID; 1157402; -.
DR   KEGG; xac:XAC3331; -.
DR   PATRIC; 24058797; VBIXanAxo33670_3450.
DR   eggNOG; COG0155; -.
DR   HOGENOM; HOG000218418; -.
DR   KO; K00381; -.
DR   OMA; ELHQEAY; -.
DR   ProtClustDB; PRK13504; -.
DR   BioCyc; XAXO190486:GH55-3331-MONOMER; -.
DR   UniPathway; UPA00140; UER00207.
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:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.480.10; -; 2.
DR   HAMAP; MF_01540; CysI; 1; -.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF55124; SSF55124; 2.
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    568       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000388527.
FT   METAL       425    425       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       431    431       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       470    470       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       474    474       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       474    474       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   568 AA;  62418 MW;  4E86EDBFF11AE961 CRC64;
     MSHSVEDIKS ESRRLRGSLE QSLADAVTGA LREDDQTLIK YHGSYQQDDR DIRDERRRQK
     LEPAYQFMIR TRTPGGVITP TQWLALDGIA TRYANHSLRI TTRQAFQFHG VIKRELKATM
     QAINATLIDT LAACGDVNRN VQVAANPLLS QAHATLYADA ARVSEHLLPN TRAYYEIWLD
     EERVSGSGSE DEPIYGERYL PRKFKIGFAA PPLNDVDVFA NDLGFIAILR DGQLLGYNVS
     IGGGMGASHG DAETWPRVAN VIGFVTREQL LDIATAVVTT QRDFGNRAVR KRARFKYTID
     DHGLDTIVAE IARRAGFALQ PAQPFAFDHN GDRYGWVEGE DGLWHLTLSL PAGRIADTDT
     AAHLSGLRAI AQLNVGEFRM TPNQNLVIAG VLASERARVD ALVAHYGLDA GNQSATALAR
     GAMACVALPT CGLAMAEAER YLPDFGAALQ PLLQQHGLAE TPIVLRLSGC PNGCSRPYLA
     EIALVGKAPG RYNLMLGGDR RGQRLNTLYR ENITEPEILA ALEPLLARYA AERDHANDEG
     FGDFLHRAGV IALPPYPTHR RLDLELLA
//