ID CYSI_BLOPB Reviewed; 575 AA. AC Q493N3; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 24. 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=BPEN_164; OS Blochmannia pennsylvanicus (strain BPEN). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=291272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16077009; DOI=10.1101/gr.3771305; RA Degnan P.H., Lazarus A.B., Wernegreen J.J.; RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel RT evolutionary trends among bacterial mutualists of insects."; RL Genome Res. 15:1023-1033(2005). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000016; AAZ40804.1; -; Genomic_DNA. DR RefSeq; YP_277677.1; -. DR GeneID; 3563110; -. DR GenomeReviews; CP000016_GR; BPEN_164. DR KEGG; bpn:BPEN_164; -. DR HOGENOM; Q493N3; -. DR OMA; Q493N3; TRQAFQM. DR BioCyc; CBLO291272:BPEN_164-MON; -. 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 1 575 Sulfite reductase [NADPH] hemoprotein FT beta-component. FT /FTId=PRO_0000292959. FT METAL 439 439 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 445 445 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 484 484 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 488 488 Iron (siroheme axial ligand) (By FT similarity). FT METAL 488 488 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 575 AA; 65260 MW; CAF03E18C47DDE31 CRC64; MNRKYDNNND KNIPLLSDNE RIKKESNFLR GTIAQNLDNN LTGGFNTEDA QLIRFHGMYQ QDDRDVRVER ANQKLEPLIN MMLRCRLPGG VIMPQQWLAI DDFSEKYTLY GTIRLTTRQT FQLHGLLKPN LKNVHRLLNK LGLDSIATAG DVNRNVICTA NPMESTLHYQ VWELAKSISS YLLPKSNAYA EIWLDSKKTE STDSEPILSA TYLPRKFKIA IAIPPINDVD VHANDLSFIA IKSENTDQII GFNVLVGGGL AMTYGDITTY PRKASAFGYI STKDVLKIAE TVVTVQRDWG NRSDRRHAKT KYTLTRVGVT TFKSEVERRS GVQFHPIRPY VFTDRGDRFG WVQGIDDYWH LTLFIENGRI SNNDPHKLLK RGIAEVAQIH SGSFRLTANQ NLIISGVSKD NKLMIESTLR KYGVINDDIT PQRKASMACV AFPTCPLAMA EAERFLPKFV TKIEHIMSKY RLEKDAIILR VTGCPNSCAR AMLSEIGLTG RSIGRYNLYL GGNNIGTRIP RLYKENITEN DILNILDTTI SRWAQERNSQ ESYGDYVVRS GIVNAVINSE KDFYE //