CYSI_XANOR
ID CYSI_XANOR Reviewed; 568 AA.
AC Q8KQT8; Q5GXB7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE Short=SiR-HP;
DE Short=SiRHP;
DE EC=1.8.1.2;
GN Name=cysI; Synonyms=xcysI; OrderedLocusNames=XOO3400;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN CYSTEINE BIOSYNTHESIS, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=11967067; DOI=10.1046/j.1365-2958.2002.02862.x;
RA Shen Y., Sharma P., da Silva F.G., Ronald P.;
RT "The Xanthomonas oryzae pv. oryzae raxP and raxQ genes encode an ATP
RT sulphurylase and adenosine-5'-phosphosulphate kinase that are required for
RT AvrXa21 avirulence activity.";
RL Mol. Microbiol. 44:37-48(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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 (Probable). {ECO:0000305|PubMed:11967067}.
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;
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a blocked
CC APS- (adenosine-5'-phosphosulfate) or PAPS- (3'-phosphoadenosine-5'-
CC phosphosulfate) dependent cysteine synthesis but do retain AvrXa21
CC activity. {ECO:0000269|PubMed:11967067}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL05935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAW76654.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY056057; AAL05935.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE013598; AAW76654.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8KQT8; -.
DR SMR; Q8KQT8; -.
DR STRING; 291331.XOO3400; -.
DR EnsemblBacteria; AAW76654; AAW76654; XOO3400.
DR KEGG; xoo:XOO3400; -.
DR PATRIC; fig|291331.8.peg.3763; -.
DR HOGENOM; CLU_001975_3_2_6; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000006735; Chromosome.
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 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..568
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000388532"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 474
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"
SQ SEQUENCE 568 AA; 62400 MW; 85222256488C1BD6 CRC64;
MSHSVEDIKS ESRRLRGSLE QSLADAVTGA LREDDQTLIK YHGSYQQDDR DIRDERRQQK
LEPAYQFMIR TRTPGGVITP AQWLALDGIA TRYANHSLRI TTRQAFQFHG VIKRELKATM
QAINATLIDT LAACGDVNRN VQVAANPLLS QAHATLYADA ACVSEHLLPN TRAYYEIWLD
EERVSGSGNE DEPIYGDRYL PRKFKIGFAA PPLNDVDVFA NDLGFIAILR DGRLLGYNVS
IGGGMGASHG DAQTWPRVAN VIGFVTRDQL LDIATAVVTT QRDFGNRAVR KRARFKYTID
DHGLDTIVAE IARRAGFALQ PAQPFAFEHN GDRYGWVEGE DGLWHLTLSL PAGRIADTDT
ATHLSGLRAI AQLNVGEFRM TPNQNLVIAG VPASERARVD ALVAQYALDA GNRSASALAR
GAMACVALPT CGLAMAEAER YLPDFSAALQ PLLQQHGLAD TPIVLRLSGC PNGCSRPYLA
EIALVGKAPG RYNLMLGGDR RGQRLNTLYR ENITEPEILA ALEPLLARYA AERDHANDEG
FGDFLHRAGL IALPSYPTHR RLDLELLA
