ID A0A3R9ZZV0_9BACL Unreviewed; 573 AA.
AC A0A3R9ZZV0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000256|HAMAP-Rule:MF_01540};
DE Short=SiR-HP {ECO:0000256|HAMAP-Rule:MF_01540};
DE Short=SiRHP {ECO:0000256|HAMAP-Rule:MF_01540};
DE EC=1.8.1.2 {ECO:0000256|HAMAP-Rule:MF_01540};
GN Name=cysI {ECO:0000256|HAMAP-Rule:MF_01540,
GN ECO:0000313|EMBL:RTE02860.1};
GN ORFNames=EJQ19_28825 {ECO:0000313|EMBL:RTE02860.1};
OS Paenibacillus whitsoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496558 {ECO:0000313|EMBL:RTE02860.1, ECO:0000313|Proteomes:UP000276128};
RN [1] {ECO:0000313|EMBL:RTE02860.1, ECO:0000313|Proteomes:UP000276128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MER 54 {ECO:0000313|EMBL:RTE02860.1,
RC ECO:0000313|Proteomes:UP000276128};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT spacecraft assembly.";
RL Submitted (DEC-2018) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01540};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01540};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01540};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01540};
CC Note=Binds 1 siroheme per subunit. {ECO:0000256|HAMAP-Rule:MF_01540};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01540}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429, ECO:0000256|HAMAP-
CC Rule:MF_01540}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RTE02860.1}.
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DR EMBL; RXHU01000110; RTE02860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9ZZV0; -.
DR OrthoDB; 9803707at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000276128; Unassembled WGS sequence.
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; 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 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01540};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01540};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01540};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01540};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01540}; Reference proteome {ECO:0000313|Proteomes:UP000276128}.
FT DOMAIN 75..137
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 171..332
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 356..419
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT BINDING 438
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 444
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 483
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 487
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 487
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:0000256|HAMAP-Rule:MF_01540"
SQ SEQUENCE 573 AA; 64931 MW; 02FCF0F2942F144B CRC64;
MSENNLLSKN SAPHSDVEAI KIRSNYLRGS LEETLQDRIT GSIPEDDNRL MKFHGSYMQD
DRDLRNERQK QKLEPAYQFM LRVRAAGGVV TSDQWLMMDR IAQRYANGTI RLTTRQSFQL
HGVLKWNMKK TIQEVNASLL STLAACGDVN RNVMCNPNPH QSEIHGEVYE WASKISAHLD
PHTRAYHEIW LDEEKVIDSR SEEEQEPIYG KVYLPRKFKI GIAVPPSNDV DVFSQDLGYI
AIVENGKLIG FNVSVGGGMG MSHGDTKTYP QVAQVIGFCT PEQVIDVAEK TVTIQRDYGD
RSVRKHARFK YTIDDRGIDW FIGELHARLG WKLEAPRAYH FDNNGDRYGW VKGVGGKWHF
TLFIQNGRVK DEGSYRLMTG LREIAKIHNG DFRLTSNQNL IIGNVSAQKK KKIEEMIAEY
GLTDGMHYSA LRRSSMACVA LPTCGLAMAE SERYLPSLID KIEPLLEENG LRDEEIVIRM
TGCPNGCARP MLAELSFIGK AAGKYNMYLG GAHNGSRLNK MYKENIGEAE IMDSLRTIIP
HYAKERNKGE HFGDFVIRAG YVKEVRSGQD FHA
//
