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Database: UniProt
Entry: A0A2G1XNS3_STRCJ
LinkDB: A0A2G1XNS3_STRCJ
Original site: A0A2G1XNS3_STRCJ 
ID   A0A2G1XNS3_STRCJ        Unreviewed;       865 AA.
AC   A0A2G1XNS3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE            EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN   ORFNames=BLA24_04675 {ECO:0000313|EMBL:PHQ52866.1}, CYQ11_28855
GN   {ECO:0000313|EMBL:PPT11474.1};
OS   Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ52866.1, ECO:0000313|Proteomes:UP000222531};
RN   [1] {ECO:0000313|EMBL:PHQ52866.1, ECO:0000313|Proteomes:UP000222531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ52866.1,
RC   ECO:0000313|Proteomes:UP000222531};
RX   PubMed=29053243;
RA   Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT   "Identification of the Biosynthetic Pathway for the Antibiotic
RT   Bicyclomycin.";
RL   Biochemistry 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:PPT11474.1, ECO:0000313|Proteomes:UP000239771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT11474.1,
RC   ECO:0000313|Proteomes:UP000239771};
RA   Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT   "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT   bacterial classes.";
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=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRNR:PIRNR037149};
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:PHQ52866.1}.
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DR   EMBL; NHZO01000070; PHQ52866.1; -; Genomic_DNA.
DR   EMBL; PKFQ01000002; PPT11474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1XNS3; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000222531; Unassembled WGS sequence.
DR   Proteomes; UP000239771; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
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   InterPro; IPR041575; Rubredoxin_C.
DR   NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW   ECO:0000256|PIRNR:PIRNR037149};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222531};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          12..295
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..391
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          429..476
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          568..629
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          640..776
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   REGION          840..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  90846 MW;  61D7700E9B85CCBD CRC64;
     MTPSAPATER RRLVLVGHGM VGQRFLEALY EQEDAARWQV TVLAEEPRPA YDRVHLTSAF
     TGTSPEELSL CDREFLSRHG IDLRLGDPVV AVDREARRVT CASGGEVPYD ALVLATGSYP
     FVPPVPGHDA PGCHVYRTVD DVAAIQARAA GARTGAVVGG GLLGLEAAGA LRAMGLDTHV
     VEFAPRLMAL QVDDAGGALL RQKIEQLGVT VHTGAGATSI DTGPDGEVVA MTLSDGTSFA
     TDLVVFSAGV RPQDRLARDC GLPVGERGGI TVDARCRTAD PHVWAVGECA RAVDGTVYGL
     VAPGYAMAET AARDLCGGSG EFTGADTSTK LKLLGVDVAS FGDAHGATEG ALDVTYADSR
     AGVYKKLVVG ADGSLLGGVL VGDADAYATL RPLAGNGRPL TVPAEQLLLP AAAGPAGATG
     GAALPEDAIV CSCHNVDKAT IRSAVTEGVC ASVAAVKKCT KAGTGCGSCE KLLTTLVDDE
     LAATGVAAAR GLCEHFAHTR AELYEIIRVK GITTFTRLLA EHGTGEGCAV CKPVVASILA
     TLGDTSHILD GEQAALQDTN DHFLANLQRN GSYSVVPRVP GGEITPDGLI TIGAIARDFG
     LYTKITGGQR IDMFGATVDQ LPAIWRRLVD AGFESGHAYG KALRTVKSCV GQTWCRYGVQ
     DSVALAIELE LRYRGLRAPH KIKSAVSGCA RECAEARSKD FGVIATAEGW NLYVGGNGGM
     TPRHADLLLQ DADHDTLVRT VDRFLMFYIR TADRLERTAP WIERLEGGLD HLRAVIVDDA
     LGIAADLDAQ MARHIARYED EWAATLADPE RLRRFASFVN APGTPDPTVR FTPERAQIRP
     ARVGEDPLPG PVTAGAGPAP KVRIR
//
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