CYSI_NITWN
ID CYSI_NITWN Reviewed; 576 AA.
AC Q3SV33;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Nwi_0591;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA03858.1; -; Genomic_DNA.
DR RefSeq; WP_011313919.1; NC_007406.1.
DR AlphaFoldDB; Q3SV33; -.
DR SMR; Q3SV33; -.
DR STRING; 323098.Nwi_0591; -.
DR EnsemblBacteria; ABA03858; ABA03858; Nwi_0591.
DR KEGG; nwi:Nwi_0591; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_2_5; -.
DR OMA; MGMTHGD; -.
DR OrthoDB; 1588103at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000002531; Chromosome.
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-UniRule.
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; IEA:UniProtKB-UniRule.
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..576
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000388503"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 447
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 486
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 490
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 490
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; 64770 MW; 4ED812EDA4FEBA74 CRC64;
MDAKTQPDRS RDVSQPLDKL GPDETLKANS DYLRGTIKQS LADEITSAVT ANDAKLMKFF
GIYQQDDRDI RDERRRQKLE AAFSFMVRVR LPGGVCSPGQ WLKLDELARN YAGDTLRLTT
RQTFQFHRVM KHNLRSLIQG LRDILLDTRA ACGDDTRGVM STVNPDLSKL HAEVYALAKR
ASDHAVHRTG AYKEIWYEAE REQTDGPEEP FYGRTYMPRK FKIGFAIPPS NDIDVYGQDL
GFIAIAHRGK LKGFNVAIGG GLGRTDQSPK TYPRLASVIG YIDADKLFPT IDAVMSVQRD
YGDRLDRLHA RFKYTIDEKG IDWIKAETER RLGFALKPEQ PYTFTSNGDP LGWVKGEDGR
EHCALFIQNG RVINTPDHPM MDGLRAIAQV HKGMFRVTPN QNLIIADIAS RDRPEIEALM
KEYGLDQFET RSGLRLNSMA CVALPTCGLA MAESERYLPD LLTKIEAILN TYGLTDDPIT
IRMTGCPNGC ARPYIAEIGL TGRAPGKYNL YLGGGFHGER LNKMYLENVG EPAILEALDK
TLGHYARDRK PGEHFGDFAI RAGYVVEVKE GRFFND
