CYSI_PAESJ
ID CYSI_PAESJ Reviewed; 574 AA.
AC C6CXN6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Pjdr2_1787;
OS Paenibacillus sp. (strain JDR-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=324057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDR-2;
RX PubMed=22675593; DOI=10.4056/sigs.2374349;
RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M.,
RA Pati A., Martin J., Copeland A., Land M.L., Goodwin L., Jones J.B.,
RA Ingram L.O., Shanmugam K.T., Preston J.F.;
RT "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL Stand. Genomic Sci. 6:1-10(2012).
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; CP001656; ACT00449.1; -; Genomic_DNA.
DR RefSeq; WP_015843394.1; NC_012914.1.
DR AlphaFoldDB; C6CXN6; -.
DR SMR; C6CXN6; -.
DR STRING; 324057.Pjdr2_1787; -.
DR EnsemblBacteria; ACT00449; ACT00449; Pjdr2_1787.
DR KEGG; pjd:Pjdr2_1787; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_2_9; -.
DR OMA; MGMTHGD; -.
DR OrthoDB; 1588103at2; -.
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: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.
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..574
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000388509"
FT BINDING 439
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 445
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 488
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 488
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 574 AA; 64063 MW; CF6D2DCED03D93E7 CRC64;
MAKNHKVEPV GGPPSDVEHL KLESNYLRGS LTDSLANRIT GGLPDLDNRL LKFHGSYMQD
DRDYRNEREK QKLEPYYQFM LRVVTPGGVA TPEQWLLMDS LADKYGTGSL KLTTRQAFQL
HGVLKWNLKK TIQEINAAML STLAACGDVS RNVMCNPNPY QSELHSEVFH WSQQLTSHLA
PKTPAYHEIW LDGEKVVDGA EQGEVEPIYG PVYLPRKFKI GIAVPPSNDV DVYSQDLGYI
AILGEDGKLA GFNVCVGGGM GMTHGDTATY PQLAKVIGFV TPDQVLDLAE KVVTIQRDYG
NRSVRKYARF KYTIDRHGLP WFMDELQDRL GWELAPAREF HFEHTGDRYG WIKGKDGKWN
LNLYVQAGRV VDTEDNKLRS ALREIAKIHT GDFRLTANQN LVIANVTAQK KTKIVALLKE
FGIAEGSNYS ALRRSALSCV ALPTCGLAMA EAERYLPSLI DRLEPILANA GLQDQEINIR
MTGCPNGCAR PALGEISFIG KSPGKYNMYM GAGFTGDRLS KMYKENIGED EIIDTLTPII
DRYASERNKG ENFGDFVIRA GYVKAVTDGT NFHD
