(data stored in ACNUC7421 zone)

SWISSPROT: CYSI_PSEHT

ID   CYSI_PSEHT              Reviewed;         565 AA.
AC   Q3IFM1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000255|HAMAP-Rule:MF_01540};
DE            Short=SiR-HP {ECO:0000255|HAMAP-Rule:MF_01540};
DE            Short=SiRHP {ECO:0000255|HAMAP-Rule:MF_01540};
DE            EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01540};
GN   Name=cysI {ECO:0000255|HAMAP-Rule:MF_01540};
GN   OrderedLocusNames=PSHAa0155;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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. {ECO:0000255|HAMAP-Rule:MF_01540}.
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH. {ECO:0000255|HAMAP-Rule:MF_01540}.
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01540};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01540};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01540};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01540};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC       hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01540}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein. {ECO:0000255|HAMAP-
CC       Rule:MF_01540}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family. {ECO:0000255|HAMAP-Rule:MF_01540}.
DR   EMBL; CR954246; CAI85259.1; -; Genomic_DNA.
DR   RefSeq; WP_011326874.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFM1; -.
DR   SMR; Q3IFM1; -.
DR   STRING; 326442.PSHAa0155; -.
DR   EnsemblBacteria; CAI85259; CAI85259; PSHAa0155.
DR   KEGG; pha:PSHAa0155; -.
DR   PATRIC; fig|326442.8.peg.149; -.
DR   eggNOG; ENOG4105ET1; Bacteria.
DR   eggNOG; COG0155; LUCA.
DR   HOGENOM; HOG000218418; -.
DR   KO; K00381; -.
DR   OMA; GKYNMYL; -.
DR   OrthoDB; POG091H04FQ; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000006843; Chromosome I.
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-EC.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
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; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF55124; SSF55124; 2.
DR   TIGRFAMs; TIGR02041; CysI; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFM1.
DR   SWISS-2DPAGE; Q3IFM1.
KW   4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    565       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292962.
FT   METAL       429    429       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01540}.
FT   METAL       435    435       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01540}.
FT   METAL       474    474       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01540}.
FT   METAL       478    478       Iron (siroheme axial ligand).
FT                                {ECO:0000255|HAMAP-Rule:MF_01540}.
FT   METAL       478    478       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01540}.
SQ   SEQUENCE   565 AA;  62933 MW;  F622A443A6723502 CRC64;
     MSEQDKNVKL SDNERMKRES NFLRGTIATD LKDEITGGFT ADNFQLIRFH GMYQQDDRDI
     RGERAKQKLE PLHNVMLRAR MPGGIIKPEQ WLAIDKFAEE KTSYGSIRLT TRQTFQFHGV
     LKPNIKGMHQ LLDSVGIDSI ATAGDVNRNV LCTTNPVESE LHQEAYEWAA KISEHLLPKT
     KAYAEIWLNG EKAETTEEPI LGSNYLPRKF KTTVTIPPNN EVDVHANDLN FVAIAENGKL
     IGFNVLVGGG LAMTHGDTAT YPRKADDFGF IPLEHTLKIA EHVVSVQRDW GNRSNRKNAK
     TKYTLDRVGV DVFKAEVEKR AGVEFASSRP YKFTHRGDRI GWVEGIDGKH HLTLFIQSGR
     ILDYPDKPLK TGCRKIAEVH QGDMRMTANQ NLIIAGVAAN QKAVIEEIAR NHGLIDDKDT
     EQRKNSMACV ALPTCPLAMA EAERYLPSLV EKIEALLAKH GVPNDSIIMR VVGCPNGCGR
     AMLAEAGLVG KGPGKYNVYL GGNLEGTRIP KLYLENVGED VYLAAFDELI GQWVNERNDG
     ECFGDFVIRK GIVAEVKVSV TDFHA
//

If you have problems or comments...

PBIL Back to PBIL home page