ID CYSI_VIBF1 Reviewed; 576 AA. AC Q5E840; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 25-NOV-2008, 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=VF_0311; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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; CP000020; AAW84806.1; -; Genomic_DNA. DR RefSeq; YP_203694.1; -. DR GeneID; 3277269; -. DR GenomeReviews; CP000020_GR; VF_0311. DR KEGG; vfi:VF0311; -. DR NMPDR; fig|312309.3.peg.311; -. DR HOGENOM; Q5E840; -. DR BioCyc; VFIS312309:VF0311-MON; -. DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP 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 1 576 Sulfite reductase [NADPH] hemoprotein FT beta-component. FT /FTId=PRO_0000199913. FT METAL 439 439 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 445 445 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 485 485 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 489 489 Iron (siroheme axial ligand) (By FT similarity). FT METAL 489 489 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 576 AA; 64631 MW; DEC6E859BAF9FD3C CRC64; MSELIDVKTI LSGTELGPLA DNERLKRESK YLRGTIVEDL QDRITGGFTK DNFQLIRFHG MYQQDDRDIR AERAKQKLEP LHNVMLRARM PGGIITPKQW LAIDKFAEEH TSYGSLRLTT RQTFQFHGVL KPNIKLMHQT LNSIGIDSIA TAGDVNRNVL CTTNPVESEL HQEAYEWAKK ISEHLLPKTR AYAEIWLDGE KLETTDEEPI LGSNYLPRKF KTTVVIPPQN DVDVHANDLN FIAIADNGKL VGFNVLVGGG LAMTHGDTAT YPRKADDFGF VPLDKTLDVA AAVVTTQRDW GNRSNRKNAK TKYTLDRVGS DVFKGEVEKR AGVQFEKSRP YELTERGDRI GWVEGIDGKH HLALFIENGR LLDYPGKPLK TGVAEIAKVH QGDFRMTANQ NLIVAGVPSE QKDHIEQIAR AHGLIDDTHS EQRKNSMACV AFPTCPLAMA EAERFLPEFV TEIEGVLKKH NLPEEDNIIF RVTGCPNGCG RAMLAEIGLV GKAPGRYNFH LGGNRSGTRV PKMYKENITD RQILTEIDQL VGRWATERNE NEGFGDFTIR AGIVDEVKVS KRDFHA //