SIR_MAIZE
ID SIR_MAIZE Reviewed; 635 AA.
AC O23813;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sulfite reductase [ferredoxin], chloroplastic;
DE Short=ZmSiR;
DE EC=1.8.7.1 {ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:10712553};
DE Flags: Precursor;
GN Name=SIR;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf;
RA Ideguchi T., Akashi T., Onda Y., Hase T.;
RT "cDNA cloning and functional expression of ferredoxin-dependent sulfite
RT reductase from maize in E. coli cells.";
RL (In) Mathis P. (eds.);
RL Research in Photosynthesis from Light to Biosphere II, pp.713-716, Kluwer,
RL Amsterdam (1995).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16663524; DOI=10.1104/pp.74.4.866;
RA Schmutz D., Brunold C.;
RT "Intercellular localization of assimilatory sulfate reduction in leaves of
RT Zea mays and Triticum aestivum.";
RL Plant Physiol. 74:866-870(1984).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH
RP FERREDOXIN.
RX PubMed=10506201; DOI=10.1074/jbc.274.41.29399;
RA Akashi T., Matsumura T., Ideguchi T., Iwakiri K., Kawakatsu T.,
RA Taniguchi I., Hase T.;
RT "Comparison of the electrostatic binding sites on the surface of ferredoxin
RT for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and
RT sulfite reductase.";
RL J. Biol. Chem. 274:29399-29405(1999).
RN [4]
RP MUTAGENESIS OF ARG-193; LYS-276 AND LYS-278, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND REVIEW.
RX PubMed=11132635; DOI=10.1016/s0162-0134(00)00138-0;
RA Nakayama M., Akashi T., Hase T.;
RT "Plant sulfite reductase: molecular structure, catalytic function and
RT interaction with ferredoxin.";
RL J. Inorg. Biochem. 82:27-32(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Golden cross Bantam T51;
RX PubMed=10712553; DOI=10.1104/pp.122.3.887;
RA Yonekura-Sakakibara K., Onda Y., Ashikari T., Tanaka Y., Kusumi T.,
RA Hase T.;
RT "Analysis of reductant supply systems for ferredoxin-dependent sulfite
RT reductase in photosynthetic and nonphotosynthetic organs of maize.";
RL Plant Physiol. 122:887-894(2000).
RN [6]
RP FUNCTION.
RX PubMed=11163356; DOI=10.1016/s0014-5793(00)02342-5;
RA Sato N., Nakayama M., Hase T.;
RT "The 70-kDa major DNA-compacting protein of the chloroplast nucleoid is
RT sulfite reductase.";
RL FEBS Lett. 487:347-350(2001).
RN [7]
RP FUNCTION, MUTAGENESIS OF ARG-193, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14871491; DOI=10.1016/j.bbabio.2003.11.004;
RA Hirasawa M., Nakayama M., Hase T., Knaff D.B.;
RT "Oxidation-reduction properties of maize ferredoxin: sulfite
RT oxidoreductase.";
RL Biochim. Biophys. Acta 1608:140-148(2004).
RN [8]
RP INHIBITORS.
RX PubMed=16307304; DOI=10.1007/s11120-005-6966-y;
RA Hirasawa M., Nakayama M., Kim S.-K., Hase T., Knaff D.B.;
RT "Chemical modification studies of tryptophan, arginine and lysine residues
RT in maize chloroplast ferredoxin:sulfite oxidoreductase.";
RL Photosyn. Res. 86:325-336(2005).
RN [9]
RP INTERACTION WITH FERREDOXIN, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16469743; DOI=10.1074/jbc.m510530200;
RA Saitoh T., Ikegami T., Nakayama M., Teshima K., Akutsu H., Hase T.;
RT "NMR study of the electron transfer complex of plant ferredoxin and sulfite
RT reductase: mapping the interaction sites of ferredoxin.";
RL J. Biol. Chem. 281:10482-10488(2006).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17371503; DOI=10.1111/j.1742-4658.2007.05748.x;
RA Sekine K., Fujiwara M., Nakayama M., Takao T., Hase T., Sato N.;
RT "DNA binding and partial nucleoid localization of the chloroplast stromal
RT enzyme ferredoxin:sulfite reductase.";
RL FEBS J. 274:2054-2069(2007).
CC -!- FUNCTION: Essential protein with sulfite reductase activity required in
CC assimilatory sulfate reduction pathway during both primary and
CC secondary metabolism and thus involved in development and growth.
CC {ECO:0000269|PubMed:10712553, ECO:0000269|PubMed:11163356,
CC ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:17371503}.
CC -!- FUNCTION: DNA-binding protein that binds to both double-stranded and
CC single-stranded DNA without significant sequence specificity to
CC reversibly repress the transcriptional activity of chloroplast
CC nucleoids by promoting DNA compaction and possibly regulate DNA
CC replication. {ECO:0000269|PubMed:11163356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:10712553};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by the tryptophan-modifying reagent, N-
CC bromosuccinimide (NBS), by the lysine-modifying reagent, N-
CC acetylsuccinimide and by the arginine-modifying reagent, phenylglyoxal.
CC Complex formation with ferredoxin prevents these inhibitions.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 uM for ferredoxin {ECO:0000269|PubMed:10506201,
CC ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491,
CC ECO:0000269|PubMed:16469743};
CC KM=1 mM for nitrite {ECO:0000269|PubMed:10506201,
CC ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491,
CC ECO:0000269|PubMed:16469743};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10506201,
CC ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491,
CC ECO:0000269|PubMed:16469743};
CC Redox potential:
CC E is -285 +/- 5 mV for siroheme and -400 +/- 5 mV for 2Fe-2S at pH
CC 7.5. {ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:11132635,
CC ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:16469743};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ferredoxin.
CC {ECO:0000250, ECO:0000269|PubMed:10506201,
CC ECO:0000269|PubMed:16469743}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast
CC nucleoid. Plastid, chloroplast stroma. Plastid stroma.
CC -!- TISSUE SPECIFICITY: Present in roots and leaves (at protein level). In
CC leaves, sulfite reductase activity is detected in both bundle sheath
CC and mesophyll cell types. {ECO:0000269|PubMed:10712553,
CC ECO:0000269|PubMed:16663524}.
CC -!- PTM: Phosphorylated; this phosphorylation reduces DNA-binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; D50679; BAA23641.1; -; mRNA.
DR PIR; T01695; T01695.
DR PDB; 5H8V; X-ray; 2.20 A; A/B=53-635.
DR PDB; 5H8Y; X-ray; 2.20 A; A/B/C/D=53-635.
DR PDB; 5H92; X-ray; 2.08 A; A/B=53-635.
DR PDBsum; 5H8V; -.
DR PDBsum; 5H8Y; -.
DR PDBsum; 5H92; -.
DR AlphaFoldDB; O23813; -.
DR SMR; O23813; -.
DR STRING; 4577.GRMZM2G090338_P01; -.
DR PaxDb; O23813; -.
DR PRIDE; O23813; -.
DR MaizeGDB; 275273; -.
DR eggNOG; KOG0560; Eukaryota.
DR BRENDA; 1.8.7.1; 6752.
DR SABIO-RK; O23813; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O23813; baseline and differential.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:CAFA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IDA:UniProtKB.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CAFA.
DR GO; GO:1900160; P:plastid chromosome packaging; IDA:CAFA.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR GO; GO:0019424; P:sulfide oxidation, using siroheme sulfite reductase; ISS:UniProtKB.
DR Gene3D; 3.30.413.10; -; 2.
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 InterPro; IPR011787; SiR_ferredoxin-dep.
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; TIGR02042; sir; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chloroplast; DNA-binding; Heme; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome; Thioether bond;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 51..635
FT /note="Sulfite reductase [ferredoxin], chloroplastic"
FT /id="PRO_5000139992"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 544
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:0000250"
FT MUTAGEN 193
FT /note="R->A: Loss of sulfite reductase activity, low
FT nitrite reductase activity and reduced siroheme redox
FT potential."
FT /evidence="ECO:0000269|PubMed:11132635,
FT ECO:0000269|PubMed:14871491"
FT MUTAGEN 193
FT /note="R->E: Loss of sulfite reductase activity, increased
FT nitrite reductase activity and reduced siroheme redox
FT potential."
FT /evidence="ECO:0000269|PubMed:11132635,
FT ECO:0000269|PubMed:14871491"
FT MUTAGEN 276
FT /note="K->Q: Loss of sulfite reductase activity, no nitrite
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:11132635"
FT MUTAGEN 278
FT /note="K->N: Loss of sulfite reductase activity, basal
FT nitrite reductase activity."
FT /evidence="ECO:0000269|PubMed:11132635"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:5H92"
FT TURN 75..80
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5H8V"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:5H92"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 205..220
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5H92"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 486..490
FT /evidence="ECO:0007829|PDB:5H92"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 508..525
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 550..558
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:5H92"
FT STRAND 577..584
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 588..602
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:5H92"
FT HELIX 618..628
FT /evidence="ECO:0007829|PDB:5H92"
SQ SEQUENCE 635 AA; 70015 MW; 759B0564472E163B CRC64;
MSGAIGGAEV HGFRGAAAQL PRSRVLGRPI RVAPPAAARP GGASAGSIRA VSAPAKKDAS
EVKRSKVEII KEKSNFLRYP LNEELVSEAP NINESAVQLI KFHGSYQQTD RDVRGQKNYS
FMLRTKNPCG KVPNQLYLAM DTLADEFGIG TLRLTTRQTF QLHGVLKKNL KTVLSTVIKN
MGSTLGACGD LNRNVLAPAA PYVKKDILFA QQTAENIAAL LTPQSGAYYD LWVDGEKIMS
AEEPPEVTKA RNDNSHGTNF PDSPEPIYGT QYLPRKFKVA VTAAGDNSVD ILTNDIGVVV
VSDDAGEPIG FNIYVGGGMG RTHRVETTFP RLADPLGYVP KEDILYAIKA IVVTQRENGR
RDDRKYSRMK YMIDRWGIDR FRAEVEKYYG KKFESFRPLP EWQFNSYLGW QEQGDGKLFY
GVHVDNGRVG GQAKKTLREI IEKYNLDVSI TPNQNLILCG IDQAWREPIT TALAQAGLLE
PKDVDPLNLT AMACPALPLC PLAQTEAERG ILPILKRIRA VFNKVGIKDS ESVVVRITGC
PNGCARPYMA ELGFVGDGPK SYQIWLGGTP NQSTLAESFM DKVKLDDIEK VLEPLFTYWN
GTRQEGESFG SFTNRTGFDK LKEVVNKWAE SPSAA
