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CYSI_XANCP
ID   CYSI_XANCP              Reviewed;         568 AA.
AC   Q8P608;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; OrderedLocusNames=XCC3174;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
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., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC       6-electron reduction of sulfite to sulfide. This is one of several
CC       activities required for the biosynthesis of L-cysteine from sulfate.
CC       {ECO:0000255|HAMAP-Rule:MF_01540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC         sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-
CC         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-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; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01540}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01540}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000255|HAMAP-Rule:MF_01540}.
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DR   EMBL; AE008922; AAM42444.1; -; Genomic_DNA.
DR   RefSeq; NP_638520.1; NC_003902.1.
DR   RefSeq; WP_011038281.1; NC_003902.1.
DR   AlphaFoldDB; Q8P608; -.
DR   SMR; Q8P608; -.
DR   STRING; 340.xcc-b100_1003; -.
DR   EnsemblBacteria; AAM42444; AAM42444; XCC3174.
DR   KEGG; xcc:XCC3174; -.
DR   PATRIC; fig|190485.4.peg.3390; -.
DR   eggNOG; COG0155; Bacteria.
DR   HOGENOM; CLU_001975_3_2_6; -.
DR   OMA; MGMTHGD; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IBA:GO_Central.
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:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR   Gene3D; 3.30.413.10; -; 2.
DR   HAMAP; MF_01540; CysI; 1.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   PANTHER; PTHR11493; PTHR11493; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF55124; SSF55124; 2.
DR   SUPFAM; SSF56014; SSF56014; 2.
DR   TIGRFAMs; TIGR02041; CysI; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW   Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Sulfite reductase [NADPH] hemoprotein beta-
FT                   component"
FT                   /id="PRO_0000388528"
FT   BINDING         425
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         431
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         470
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         474
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         474
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
SQ   SEQUENCE   568 AA;  62565 MW;  130DF10005619537 CRC64;
     MTHSVEDIKS TSRRLRGSLE QSLADPVTGA LREDDQTLIK YHGSYQQDDR DIRDERRRQK
     LEPAYQFMIR TRTPGGVISP SQWLALDGIA TRYANHSLRI TTRQAFQFHG VIKRELKATM
     QAINATLIDT LAACGDVNRN VQVAANPLRS QAHATLYADA ARVSEHLLPN TRAYYEIWLD
     EERVSGSGAE DEPIYGDRYL PRKFKIGFAA PPHNDVDVFA NDLGFIAILR EGQLLGYNVS
     IGGGMGASHG DAETWPRVAN VIGFVTGDQL LDIATAVVTT QRDLGNRAVR KRARFKYTID
     DHGLDTIVAE IERRAGFSLQ PAQPFAFAHN GDRYGWVEGE QGDWHLTLSL PAGRIADTDT
     AAHLSGLRAI AQLQMGEFRM TPNQNLVIAG VPAEQRAQID QLVAQYGLDA GNLAPTALAR
     GAMACVALPT CGLAMAEAER YLPDFSAALQ PLLERHGLAQ TPIVLRLSGC PNGCSRPYLA
     EIALVGKAPG RYNLMLGGDR RGQRLNTLYR ENINEADILA ALEPLLARYA AERDRHTDEG
     FGDFLHRSGL IALPPYPTHR HLDLELLA
 
 
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