CYSI_NITOC
ID CYSI_NITOC Reviewed; 579 AA.
AC Q3JBJ1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Noc_1306;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(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; CP000127; ABA57805.1; -; Genomic_DNA.
DR RefSeq; WP_002809703.1; NC_007484.1.
DR AlphaFoldDB; Q3JBJ1; -.
DR SMR; Q3JBJ1; -.
DR STRING; 323261.Noc_1306; -.
DR EnsemblBacteria; ABA57805; ABA57805; Noc_1306.
DR KEGG; noc:Noc_1306; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_2_6; -.
DR OMA; MGMTHGD; -.
DR OrthoDB; 1588103at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000006838; 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..579
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000388504"
FT BINDING 434
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 440
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 479
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 483
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 483
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 579 AA; 65679 MW; 9F31A17304306DFD CRC64;
MTHDLQQKSK LSAVEKIKAK SRYLRGTIQE GLADLATGAV VEEDTKLLKF HGTYQQDDRD
LRTERMRQKL EPAYSFMVRV RMPGGVCMPK QWLQLDELAR KYANNSLRIT TRQTFQFHSV
VKRHLRSTIA GINEALLSTI AACGDVNRNV VCHNNPYLSP LHKTVYEWSK RLSNHFLPQT
QAYHEIWMGK EKVAGTLPEN EEPIYGETYL PRKFKIGITI PPNNEIDVFS QDLGLIAIAK
GSRLVGFNIC VGGGMGMTHS EPSTYPRLGD VIGFCTPSQL LEVAENILKI QRDFGNRCDR
KQARLKYTID SRSIDWFKAE LNQRLGWDLE PARPFHFESN GDHFGWVEDS KGRWHLTLFL
LSGRIKDTLD QPLMTGLREI AKIHKGDFRL TTNQNLTIAN ISKTNKPRIE ALLEKYRIPM
PERFSPIRQH AMSCVALPSC GLAMAESERM LPGFLARLEA VVEKAGLADE PITLRVTGCP
NGCSRPYISE IALVGKSLGR YNLYLGAGFA GQRLNKLYRE SLTEDEIIAT LSPLFEHYAR
ERQQGEHFGD FVVRAGYVDE VRAGREFHEV RSEKAVQSA
