ID A0A2N3YFC2_9MICO Unreviewed; 568 AA.
AC A0A2N3YFC2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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=ATL31_0338 {ECO:0000313|EMBL:PKW25541.1};
OS Phycicoccus duodecadis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=173053 {ECO:0000313|EMBL:PKW25541.1, ECO:0000313|Proteomes:UP000233781};
RN [1] {ECO:0000313|EMBL:PKW25541.1, ECO:0000313|Proteomes:UP000233781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12806 {ECO:0000313|EMBL:PKW25541.1,
RC ECO:0000313|Proteomes:UP000233781};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) 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:PKW25541.1}.
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DR EMBL; PJNE01000001; PKW25541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3YFC2; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000233781; 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:UP000233781};
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..321
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 345..410
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 421..561
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 61957 MW; 508344389D0A780B CRC64;
MTTTATTPRA LRPPRAGRAN GQWAVDGTAP LNANEEWKQE EGGLSVRARI EEVYSKEGFG
SIPPQDLSGR FRWWGLYTQR RPGIDGGRTA QLDDTELSDE YFMLRARLDG GALTLEQLRV
LAQISTEFAR GTADISDRQN LQYHWIRIED VPEIWRRLEA VGLQTTEACG DTPRVVLGSP
LAGIAADEII DPTPVIDEIV ERFIGDPELA NLPRKFKTAV TGHPSLDVVH EINDVSLVGV
VHPELGPGYD LWVGGGLSTA PRLAERLGTF VPEEHAAEVW HGVVRIFRDY GYRRLRAKAR
LKFLLAEWGP AEFRRVLEEE YLGYALPDGP APARATTPGD HVGVHRQKDG NHYVGAAPVV
GRVSGEVLTG LADLMADAGS GRVRFTPHQK LVVLDVAPDR LDALVSGLEA LGLSVSPSPF
RRNTIACTGI EFCKLAIVET KAAAATAITE LEQRLADVTP ALDTPISLHV NGCPNSCARV
QVADIGLKGQ LLTVDGEQVP GFQVHLGGGL ASPERDEAGL GRTMRGLKVT ADELPDLVER
LVRRFLDQRE GGETFSAWAH RVDDEVLR
//
