ID A0A365ZR66_9ACTN Unreviewed; 578 AA.
AC A0A365ZR66;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DEH69_07170 {ECO:0000313|EMBL:RBM20739.1};
OS Streptomyces sp. PT12.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1510197 {ECO:0000313|EMBL:RBM20739.1, ECO:0000313|Proteomes:UP000252839};
RN [1] {ECO:0000313|EMBL:RBM20739.1, ECO:0000313|Proteomes:UP000252839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT12 {ECO:0000313|EMBL:RBM20739.1,
RC ECO:0000313|Proteomes:UP000252839};
RA Devaraj K., Tan G.Y.A.;
RT "Diversity of actinobacteria isolated from Cape Rachado, Malaysia.";
RL Submitted (MAY-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:RBM20739.1}.
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DR EMBL; QEST01000079; RBM20739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365ZR66; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000252839; 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:UP000252839};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 114..175
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 185..336
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 362..427
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 439..575
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 63824 MW; FC3722EC3F95A7CB CRC64;
MPDSAPGSAN GPANGSANAK KPAAPGRRKA ARHRGEGQWA AGHFTPLNPN EQVKKDDDGL
NVRTRIETIY AHRGFDSIDG QDLRGRMRWW GLYTQRRPGI DGGRTAILEP EELDDEYFML
RVRIDGGQLT TAQLRVIGEI SQEFARGTAD ITDRQNIQYH WIRIEDMPEI WRRLEGVGLS
TTEACGDTPR VVLGSPVAGI AEDEIIDGTP AVEEIHRRVV GNKAYSNLPR KFKTAVSGSP
LLDVAHEIND VAFVGVVHPE LGPGFDVWVG GGLSTNPKIG VRLGAWVPLD EVADVHEGIV
GLFRDHGYRR LRTRARIKFL VADWGAERFR DVLEREYLLR RLADGPAPEQ PVAEWRDHVG
VHRQRDGRYY VGFAPRVGRV DGGTLAKIAD LAEAHGSSRV RTTVEQKMIV LDVPKDQVDA
LTDGLAALDL TTRPSTFRRG TMACTGIEFC KLAIVETKAR ATWLIEEMER RLPDFDEPLT
INVNGCPNSC ARIQIADIGL KGQLVTDADG NQVEGFQVHL GGSLGLEPGF GRKVRGLKVT
AAGLADYVER VLVRFTEQRE PGERFARWAA RADEESLS
//
