ID A0A1A3BVH6_9MYCO Unreviewed; 558 AA.
AC A0A1A3BVH6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=A5663_22055 {ECO:0000313|EMBL:OBI77406.1};
OS Mycobacterium sp. E740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834149 {ECO:0000313|EMBL:OBI77406.1, ECO:0000313|Proteomes:UP000092151};
RN [1] {ECO:0000313|Proteomes:UP000092151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E740 {ECO:0000313|Proteomes:UP000092151};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-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};
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:OBI77406.1}.
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DR EMBL; LZKP01000140; OBI77406.1; -; Genomic_DNA.
DR RefSeq; WP_068149424.1; NZ_LZKP01000140.1.
DR AlphaFoldDB; A0A1A3BVH6; -.
DR STRING; 1834149.A5663_22055; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000092151; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000092151};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 95..155
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 164..318
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 341..403
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 416..553
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 558 AA; 62285 MW; 53CDB824ECCD3FFF CRC64;
MTTTESKPAK RTRAEGQWKL GYREPLNANE QLKKDDDALN VRARILDVYS KTGFDGIDKT
DLRGRFRWMG LYTQREQGYD GTWTGDENAD LLEAKYFMMR VRCDGKALSA AALRTLGQIS
IDFARDTADI SDRMNLQYHW LEVENVPEIW ERLAAHDLQT TEACGDCPRG MLGSPLAGLS
LDEVLDPTPA LDEIVRRYIG NPEYSNLPRK YKTAISGLQD VAHEVNDISF IGVNHPEHGP
GLDLWVGGGL STNPMLAQRL GAWVPLDEVP DVWEAVTAVF RDYGYRRLRS KARLKFLIKD
WGVEKFRQVL EDEYLGRKLI DGPAPEPVKH PIDHVGIQKL KNGLNAVGVA PIAGRVSGTI
LTQVADLAEA AGSDRIRFTP YQKLIILDVP DDKVGELSTG LEALGLPPEP SHWRKNLMAC
TGIEFCKLSF TETRTRAQVL VPELEKRLED INAQLDVPIT VNINGCPNSC ARIQVADIGF
KGQMVDDGEG NSVEGFQVHL GGSLGLDSGF GRKLRQHKVL SSELGDYIDR VVRNFVKQRE
HGERFATWAL RADEADLR
//