ID A0A1I0IR05_9ACTN Unreviewed; 562 AA.
AC A0A1I0IR05;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=SAMN05421811_105132 {ECO:0000313|EMBL:SET99542.1};
OS Nonomuraea wenchangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=568860 {ECO:0000313|EMBL:SET99542.1, ECO:0000313|Proteomes:UP000199361};
RN [1] {ECO:0000313|EMBL:SET99542.1, ECO:0000313|Proteomes:UP000199361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SET99542.1,
RC ECO:0000313|Proteomes:UP000199361};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000256|ARBA:ARBA00003247}.
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:0000256|ARBA:ARBA00000993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FOHX01000005; SET99542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0IR05; -.
DR STRING; 568860.SAMN05421811_105132; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000199361; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR PROSITE; PS00365; NIR_SIR; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199361};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 99..161
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 169..323
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 347..411
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 422..558
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 62751 MW; B6164908595A9018 CRC64;
MTTPASRTPA SRHHKRPRGE GQWALGYREP LNKNEENKKN DDGLNVRQRI IDIYSKRGFD
SIDPADLRGR MRWYGLYTQR RPGIDGGKTA VLEPEELDDR YFMMRVRIDG GQLDLAQLRA
IADISNEYGR GTADITDRQN IQLHWVEIES VPDIWERLEA VGLSTTEACG DTPRVILGCP
LAGIDVDEVL DASEQIREIQ DRVIGNPAYS NLPRKFKTAL SGCPAHCTVH EINDVAFVGV
VNEHGEAGYD VWVGGGLSTN PMLAKRLGVF VRPEQAADVH EGVVGIFRDY GYRRLRHRAR
IKFLVNDWGV EKFREILETE YLKAPLPDGP APEQPRGSRR DHVGVFPQKD GNFYVGFAPK
VGRLDGDALH RIADIAERHG SGRVRTTVEQ KMVILDVAPD QVDSIVAELE AHDLQVRPST
FRRQTMACTG IEYCKLAIVE TKAAASQLID EMERRLPEFA EPLTINVNGC PNSCARIQTA
DIGLKGQLVV DENGDQVEGY QIHLGGSLGV NAGFGRKVRG LKTTAKALPD YVERVVKNFD
AQRKEGESFA DWVQRADEAD LR
//
