ID A0A1X2LXN9_9MYCO Unreviewed; 291 AA.
AC A0A1X2LXN9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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};
DE Flags: Fragment;
GN ORFNames=B8W66_07365 {ECO:0000313|EMBL:OSC41900.1};
OS Mycobacterium decipiens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC41900.1, ECO:0000313|Proteomes:UP000193247};
RN [1] {ECO:0000313|EMBL:OSC41900.1, ECO:0000313|Proteomes:UP000193247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC41900.1,
RC ECO:0000313|Proteomes:UP000193247};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OSC41900.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCXP01000005; OSC41900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2LXN9; -.
DR STRING; 1430326.B8W66_07365; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000193247; 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; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
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 PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
PE 4: Predicted;
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 96..156
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 165..290
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 291
FT /evidence="ECO:0000313|EMBL:OSC41900.1"
SQ SEQUENCE 291 AA; 32857 MW; B89F7480F67BEA90 CRC64;
MTTAHPVKTP GKTRSEGQWA LGEREPLNDS EQIKHDDAPL NVRARIENIY AKQGFDSIDK
TDLRGRFRWM GLYTQREQGY DGTWTGDENI DTIEAKYFMM RVRSDGKPMS AATLRTLGQI
STEFARDTAD IGDRENVQYH WIRIEDVPEI WDRLESVGLT TTEACGDCPR GIHGSPLAGD
SLDEVLDPSP AIDEILRRFM NNPEYANLPR KYKSAISGLQ DVSHETHDVA FVGVNHPEHG
PGMDLWVGGG LSTNPMLAQR VGVWVPLDEV PDVWEAVTKV FRDYGYRRLR A
//