ID A0A3R9V1D4_9ACTN Unreviewed; 567 AA.
AC A0A3R9V1D4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=EF918_00635 {ECO:0000313|EMBL:RSS84399.1};
OS Streptomyces sp. WAC06614.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS84399.1, ECO:0000313|Proteomes:UP000277644};
RN [1] {ECO:0000313|EMBL:RSS84399.1, ECO:0000313|Proteomes:UP000277644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC06614 {ECO:0000313|EMBL:RSS84399.1,
RC ECO:0000313|Proteomes:UP000277644};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL Submitted (NOV-2018) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSS84399.1}.
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DR EMBL; RPRY01000002; RSS84399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9V1D4; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000277644; 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; 1.
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:UP000277644};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 103..166
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 174..329
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 351..416
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 427..561
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 63365 MW; CFEF9075B6F6FEC9 CRC64;
MAETTEKPAA APAAARRKTG RHRGEGQWAV GHHTPLNGNE QFKKDDDGLN VRTRIETIYS
KTGFDSIDPN DLRGRMRWWG LYTQRKPGID GGKTAVLEPE ELDDKYFMLR VRIDGGRLTT
QQLRVIGEIS EEFARGTADI TDRQNVQYHW IRIEDVPEIW RRLEAVGLST TEACGDTPRV
ILGSPVAGIA EDEIIDGTPA IDEIYRRIVG NKDFSNLPRK FKSAISGSPL LDVAHEINDI
AFVGVEHPEH GPGFDVWVGG GLSTNPKLGV RLGTWVSLEE VPDVYEGVIS IFRDYGYRRL
RTRARLKFLV ADWGAEKFRR VLEDEYLRRK LTDGPAPQEP AGRWRDHMGV HRQRDGRFYI
GFAPRVGRVD GTILNKIADV AEQHGSGRLR TTADQKMILL DIEEARVDSA VAALEALDLR
VTPSPFRRGT MACTGIEFCK LAIVETKQRG QTLIEELERR LPDFDEPLTI NINGCPNACA
RIQVADIGLK GQLVLDDEGN QVEGYQVHLG GALGLQAGFG RKVRGLKVTK DGLPDYVERV
VKRFEAERED GERFAAWVGR ASDEALS
//
