CYSI_ECOLI
ID CYSI_ECOLI Reviewed; 570 AA.
AC P17846; Q2MA66;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
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; OrderedLocusNames=b2763, JW2733;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=B;
RX PubMed=2670946; DOI=10.1016/s0021-9258(19)84893-7;
RA Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M.,
RA Kredich N.M.;
RT "Characterization of the cysJIH regions of Salmonella typhimurium and
RT Escherichia coli B. DNA sequences of cysI and cysH and a model for the
RT siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on
RT amino acid homology with spinach nitrite reductase.";
RL J. Biol. Chem. 264:15726-15737(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-570.
RC STRAIN=K12;
RX PubMed=2005873; DOI=10.1007/bf00269864;
RA Krone F.A., Westphal G., Schwenn J.D.;
RT "Characterisation of the gene cysH and of its product phospho-
RT adenylylsulphate reductase from Escherichia coli.";
RL Mol. Gen. Genet. 225:314-319(1991).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 74-570 IN COMPLEX WITH HEME AND
RP IRON-SULFUR (4FE-4S), AND COFACTOR.
RX PubMed=7569952; DOI=10.1126/science.270.5233.59;
RA Crane B.R., Siegel L.M., Getzoff E.D.;
RT "Sulfite reductase structure at 1.6 A: evolution and catalysis for
RT reduction of inorganic anions.";
RL Science 270:59-67(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 74-570 IN COMPLEX WITH HEME AND
RP IRON-SULFUR (4FE-4S), AND COFACTOR.
RX PubMed=9315848; DOI=10.1021/bi971065q;
RA Crane B.R., Siegel L.M., Getzoff E.D.;
RT "Structures of the siroheme- and Fe4S4-containing active center of sulfite
RT reductase in different states of oxidation: heme activation via reduction-
RT gated exogenous ligand exchange.";
RL Biochemistry 36:12101-12119(1997).
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 ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848};
CC Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP-Rule:MF_01540,
CC ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540,
CC ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01540, ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848};
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA68816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M23008; AAA23651.1; ALT_INIT; Genomic_DNA.
DR EMBL; U29579; AAA69273.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75805.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76840.1; -; Genomic_DNA.
DR EMBL; Y07525; CAA68816.1; ALT_INIT; Genomic_DNA.
DR PIR; G65057; RDECSH.
DR RefSeq; NP_417243.1; NC_000913.3.
DR RefSeq; WP_001290679.1; NZ_LN832404.1.
DR PDB; 1AOP; X-ray; 1.60 A; A=74-570.
DR PDB; 2AOP; X-ray; 1.75 A; A=74-570.
DR PDB; 2GEP; X-ray; 1.90 A; A=74-570.
DR PDB; 3AOP; X-ray; 2.10 A; A=74-570.
DR PDB; 3GEO; X-ray; 2.10 A; A=74-570.
DR PDB; 4AOP; X-ray; 1.80 A; A=74-570.
DR PDB; 4G38; X-ray; 1.56 A; A=1-570.
DR PDB; 4G39; X-ray; 2.40 A; A=1-570.
DR PDB; 4GEP; X-ray; 2.00 A; A=74-570.
DR PDB; 4HTR; X-ray; 1.60 A; A=64-570.
DR PDB; 5AOP; X-ray; 2.20 A; A=74-570.
DR PDB; 5GEP; X-ray; 2.10 A; A=74-570.
DR PDB; 6C3M; X-ray; 1.50 A; A=1-570.
DR PDB; 6C3X; X-ray; 1.54 A; A=1-570.
DR PDB; 6C3Y; X-ray; 1.54 A; A=1-570.
DR PDB; 6C3Z; X-ray; 1.68 A; A=1-570.
DR PDB; 6GEP; X-ray; 1.80 A; A=74-570.
DR PDB; 7GEP; X-ray; 2.40 A; A=74-570.
DR PDB; 8GEP; X-ray; 2.20 A; A=74-570.
DR PDBsum; 1AOP; -.
DR PDBsum; 2AOP; -.
DR PDBsum; 2GEP; -.
DR PDBsum; 3AOP; -.
DR PDBsum; 3GEO; -.
DR PDBsum; 4AOP; -.
DR PDBsum; 4G38; -.
DR PDBsum; 4G39; -.
DR PDBsum; 4GEP; -.
DR PDBsum; 4HTR; -.
DR PDBsum; 5AOP; -.
DR PDBsum; 5GEP; -.
DR PDBsum; 6C3M; -.
DR PDBsum; 6C3X; -.
DR PDBsum; 6C3Y; -.
DR PDBsum; 6C3Z; -.
DR PDBsum; 6GEP; -.
DR PDBsum; 7GEP; -.
DR PDBsum; 8GEP; -.
DR AlphaFoldDB; P17846; -.
DR SASBDB; P17846; -.
DR SMR; P17846; -.
DR BioGRID; 4262276; 162.
DR ComplexPortal; CPX-5629; Sulfite reductase [NADPH] complex.
DR DIP; DIP-9380N; -.
DR IntAct; P17846; 11.
DR STRING; 511145.b2763; -.
DR DrugBank; DB02832; Siroheme.
DR jPOST; P17846; -.
DR PaxDb; P17846; -.
DR PRIDE; P17846; -.
DR EnsemblBacteria; AAC75805; AAC75805; b2763.
DR EnsemblBacteria; BAE76840; BAE76840; BAE76840.
DR GeneID; 947231; -.
DR KEGG; ecj:JW2733; -.
DR KEGG; eco:b2763; -.
DR PATRIC; fig|1411691.4.peg.3974; -.
DR EchoBASE; EB0187; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_2_6; -.
DR InParanoid; P17846; -.
DR OMA; MGMTHGD; -.
DR PhylomeDB; P17846; -.
DR BioCyc; EcoCyc:BETACOMP-MON; -.
DR BioCyc; MetaCyc:BETACOMP-MON; -.
DR BRENDA; 1.8.1.2; 2026.
DR UniPathway; UPA00140; UER00207.
DR EvolutionaryTrace; P17846; -.
DR PRO; PR:P17846; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IC:ComplexPortal.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Direct protein sequencing; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..570
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000199896"
FT BINDING 434
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:7569952,
FT ECO:0000269|PubMed:9315848"
FT BINDING 440
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:7569952,
FT ECO:0000269|PubMed:9315848"
FT BINDING 479
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:7569952,
FT ECO:0000269|PubMed:9315848"
FT BINDING 483
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:7569952,
FT ECO:0000269|PubMed:9315848"
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:0000269|PubMed:7569952,
FT ECO:0000269|PubMed:9315848"
FT CONFLICT 23
FT /note="H -> L (in Ref. 1; AAA23651)"
FT /evidence="ECO:0000305"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4G38"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4G39"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:6C3M"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2GEP"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4G39"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:6C3M"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6C3M"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6C3M"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 451..464
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:6C3M"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:4GEP"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 524..541
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 548..554
FT /evidence="ECO:0007829|PDB:6C3M"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6C3M"
SQ SEQUENCE 570 AA; 63998 MW; 03B41FEE6AB349C6 CRC64;
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ
DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAGENTIYG SIRLTNRQTF
QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH
LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI
AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDNWHLTL
FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII AGVPESEKAK IEKIAKESGL
MNAVTPQREN SMACVSFPTC PLAMAEAERF LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP
NGCGRAMLAE VGLVGKAPGR YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK
EREAGEGFGD FTVRAGIIRP VLDPARDLWD
