ID   CYSI_YERPN              Reviewed;         576 AA.
AC   Q1CLS7; C4GPQ9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   02-SEP-2026, entry version 106.
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=YPN_0721; ORFNames=YP516_0767;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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=hydrogen sulfide + 3 NADP(+) + 3 H2O = sulfite + 3 NADPH + 4
CC         H(+); 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000305; ABG17053.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000007; EEO77915.1; -; Genomic_DNA.
DR   RefSeq; WP_002209382.1; NC_008149.1.
DR   AlphaFoldDB; Q1CLS7; -.
DR   SMR; Q1CLS7; -.
DR   GeneID; 310225174; -.
DR   KEGG; ypn:YPN_0721; -.
DR   HOGENOM; CLU_001975_3_2_6; -.
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:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:TreeGrafter.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   FunFam; 3.30.413.10:FF:000003; Sulfite reductase [NADPH] hemoprotein beta-component; 1.
DR   FunFam; 3.30.413.10:FF:000004; Sulfite reductase [NADPH] hemoprotein beta-component; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 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   NCBIfam; TIGR02041; CysI; 1.
DR   NCBIfam; NF010029; PRK13504.1; 1.
DR   PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
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.
FT   CHAIN           1..576
FT                   /note="Sulfite reductase [NADPH] hemoprotein beta-
FT                   component"
FT                   /id="PRO_1000068783"
FT   BINDING         435
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         441
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         480
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         484
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT   BINDING         484
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   576 AA;  64076 MW;  28AA6EF7463B6B87 CRC64;
     MNEKHPGPLV VSGKLSDGER MKSESNFLRG TIAEDLNNGL TGGFSGDNFL LIRFHGMYQQ
     DDRDIRAERA EQKLEPRHAM MLRCRLPGGI ITPQQWLGID KFAADNTLYG SIRITNRQTF
     QFHGILKGNV KPAHQLLNEL GLDALATAND VNRNVLCTSN PVESALHQEA YEWAKKISEH
     LLPRTRAYAE IWLDAEKVAT TDEEPILGAT YLPRKFKTTV VIPPQNDVDL HANDLNFVAV
     ADKGKLIGFN VLVGGGLSIA HGDKNTYPRK ASEFGYIPLK HTLAIAEAVV TTQRDWGNRT
     DRKNAKTKYT LERVGVETFK AEVEKRAGVS FSAIKPYQFI GRGDRIGWVK GVDKKWHLTL
     FVENGRLLDY PGRSLKTGVA EIAKIHQGDF RLTANQNLIV AGVPEKDKAR IEALAREHGL
     MDDNVTSQRE NSMACVSFPT CPLAMAEAER FLPEFVTRVE GILQQHGLAD EHIVLRVTGC
     PNGCGRALLA EVGLVGKAVG RYNLHLGGNR EGTRIPRMYR ENITADEILL ITDQLVGRWA
     KERHVDEGFG DFVIRAGVIA PVIDSARDFY DVQEAM
//