ID A0A367FJ99_9ACTN Unreviewed; 560 AA.
AC A0A367FJ99;
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=DQ384_14125 {ECO:0000313|EMBL:RCG30456.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG30456.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG30456.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG30456.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-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:RCG30456.1}.
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DR EMBL; QOIL01000007; RCG30456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FJ99; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000253094; 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; 2.
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:UP000253094};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 97..159
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 167..318
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 344..410
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 420..554
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 62281 MW; DD70637D9F2A7045 CRC64;
MTSPPRPANR HHKRPRGEGQ WALGYREPLN KNEENKKNDD GLNVRQRIID VYSKRGFDSI
DPADLRGRFR WFGLYTQRKP GIDGGKTAIL EPEELDDRYF MLRVRIDGGQ LDLRQLRTIA
DIANKYARGT ADVTDRQNVQ LHWIEIESVP AIWEALEAVG LSTTEACGDT PRVMLGCPLA
GIDADEVIDA TGQIEDTVAR YIGDKAYSNL PRKFKSAMSG CPAHCTVHEI NDIAFVGVVN
EQGEKGFDLW VGGGLSTNPM LAKRLGTFVR PEQVHEVWAG VIGIFRDYGY RRLRHRARIK
FLVNDWGAER FRQVLEKEYL GYTLPDGPAP EPPRGGRRDH VGVHRQKDGN YYVGFAPKVG
RLDGDKLNLI ADIAERHGSG RVRTTVEQKM VILDVAPGEV DGLVADLEAA DLRVNPSTFR
RQTMACTGIE FCKLAIVETK ALASGLIDEL ERRLPDFTDP LTINVNGCPN SCARIQVADI
GLKGQLVTDG SGEQVEGFQI HLGGSLGVTP GFGRKVRGLK ATAAELPDYI ERVLKNFQSQ
KTDGETFAQW VERAEEADLK
//
