CYSI_ACTPL
ID CYSI_ACTPL Reviewed; 588 AA.
AC Q8VSR0; Q8VSQ9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
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};
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AP213 / Serotype 5a, and AP37 / Serotype 1;
RX PubMed=11768126;
RA Willson P.J., Gerlach G.F., Klashinsky S., Potter A.A.;
RT "Cloning and characterization of the gene coding for NADPH-sulfite
RT reductase hemoprotein from Actinobacillus pleuropneumoniae and use of the
RT protein product as a vaccine.";
RL Can. J. Vet. Res. 65:206-212(2001).
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; AF378783; AAL48202.1; -; Genomic_DNA.
DR EMBL; AF378784; AAL48203.1; -; Genomic_DNA.
DR RefSeq; WP_005599474.1; NZ_CP030753.1.
DR RefSeq; WP_009874955.1; NZ_CP026009.1.
DR AlphaFoldDB; Q8VSR0; -.
DR SMR; Q8VSR0; -.
DR STRING; 228399.appser1_19650; -.
DR GeneID; 66258634; -.
DR PATRIC; fig|416269.6.peg.1918; -.
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.
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..588
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000199892"
FT BINDING 442
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 487
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 491
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 491
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"
FT VARIANT 35
FT /note="E -> D (in strain: AP213)"
FT VARIANT 40
FT /note="G -> D (in strain: AP213)"
FT VARIANT 199
FT /note="I -> V (in strain: AP213)"
FT VARIANT 218
FT /note="F -> Y (in strain: AP213)"
FT VARIANT 250
FT /note="D -> E (in strain: AP213)"
FT VARIANT 319
FT /note="I -> V (in strain: AP213)"
FT VARIANT 373
FT /note="G -> V (in strain: AP213)"
FT VARIANT 523
FT /note="P -> S (in strain: AP213)"
SQ SEQUENCE 588 AA; 66683 MW; 4CFE8C935664B2C2 CRC64;
MSDKKIKGLE WQEKPLSDNE RLKTDSNFLR GTILEDLKDG LTGGFKGDNF QLIRFHGMYE
QDDRDIRAER LEEKLEPLKF MLLRCRLPGG IIKPYQWIEI DKFAREHTRY QSIRLTNRQT
FQYHGVPKGK LQPMHRLLHS IGLDSIATAA DMNRNVLCTS NPIESELHQQ AYEFAKKISE
HLLPRSRGYL DVWVDGKKIE SSDDLLKIED EPILGKTFLP RKFKTAVAIP PLNDVDVYAN
DLNFIAIQDD NGQLCGFNVL VGGGLSFEHG NTKTYPNVAY SLGFVPLEHT LAAAEGVVKT
QRDFGNRSDR KNARVRYTIQ NMTLDGFRAE VERCMNIKFE PTRPYEFTER GDRIGWVKGI
DNNWHLTLFI ESGRITDKPE KPLMTGVLEL AKVHKGDFRI TANQNLIVAN VAEQDKAQIE
AIARQYGLIQ EISKLRENAM SCVSLPTCPL AMAEAERVLP DFISELDKVL SKHNVADESI
ITRITGCPNG CGRAMLAEIG LVGKAIGRYN LHIGGDRAGL RIPRLYKENI TLQEIVNEID
QLVARWATER QTNEAFGDFV IRSNIIAPVV NAHIDFWDAT KIIPTTII
